Search: 1000 results found for "pdgf"

Description:

Growth and Differentiation factor 15 Mouse Recombinant

Growth/differentiation factor 15, GDF-15.

Product # :

CYT-857

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Description

GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
Growth/differentiation factor 15, GDF-15.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.
Background
What is the molecular weight/Mw of GDF15 MOUSE Protein?
GDF15 MOUSE Protein has a total Mw of 14.9kDa.

What is the source or expression system of GDF15 MOUSE Protein?
Escherichia Coli.

What is the Purity of GDF15 MOUSE Protein?
GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 MOUSE Protein?
The biological functionality of GDF15 MOUSE Protein will be determined in the future.

What is the amino acid sequence of GDF15 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

What applications can GDF15 MOUSE Protein be used in?
GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 MOUSE Protein?
The endotoxin level is minimal, GDF15 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 3 (207 a.a.) Human Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-319

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Description

TGFB3 Human Recombinant protein encoding amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag).

Source

Escherichia Coli.

Formulation

100µl purified human TGF Beta 3protein at 100µg/ml in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered clear solution.
Stability
TGF-beta 3 Human Recombinant although stable at 4°C for 1 week, should be stored at -20°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze-thaw cycles.
Applications
(a) ELISA.
(b) Western Blotting.
(c) Inhibition Assays.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Hormone Human Recombinant

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-202

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Description

GH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22kDa. Growth Hormone is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GH protein lyophilized from a 0.2µm filtered concentrated solution containing mannitol, and glycine.

Purity

Greater than 96.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the proliferation assay of rat lymphoma NB2-11 cells and was found to be less than 0.1ng/ml.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized HGH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS LVYGASDSNV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth and Differentiation Factor 15 Human Recombinant

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-335

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Description

GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.

What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Phosphogluconate Dehydrogenase, Active Human Recombinant

EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.

Product # :

ENZ-1128

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Description

PGD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483) and having a molecular mass of 55.3 kDa.PGD Human is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PGD solution (1mg/ml) contains 10% Glycerol, 1mM DTT, 0.1M NaCl, and 20mM Tris-HCl buffer (pH 8.0).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 10unit/mg. One unit will oxidize 1.0 umole of 6-phospho-D-gluconate to D-ribulose 5- phosphate per minute at pH 8.0 at 25˚C, in the presence of beta-NADP.

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Introduction
6PGD is the 2nd dehydrogenase in the pentose phosphate shift. Pentose is crucial for the biosynthesis of nucleic acid. The pentose phosphate cycle is a prominent source of NADPH. 6PGD deficiency is mostly asymptomatic, and the inheritance of this deasis is autosomal dominant. PGD deficiency elevate the erythrocyte pyruvate kinase levels of activity & decreases glutathione synthetase, which causes hemolysis.
Synonyms
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-21 Mouse Recombinant, His Tag

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-516

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Description

Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 is 100% homologous to the amino acid sequence of the Mouse FGF21 without signal sequence and contains 10 a.a. His tag at N-terminal.The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21.
Physical Appearance
Filtered white lyophilized powder.
Stability
Lyophilized FGF-21 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture. Add DTT (0.2mM) and NaCl (0.1-0.15M) before freezing to prevent potential aggregation.
Amino Acid Sequence
MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.
Background
What is the molecular weight/Mw of FGF21 MOUSE,HIS Protein?
FGF21 MOUSE,HIS Protein has a total Mw of 21.2kDa.

What is the source or expression system of FGF21 MOUSE,HIS Protein?
Escherichia Coli.

What is the Purity of FGF21 MOUSE,HIS Protein?
FGF21 MOUSE,HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21 MOUSE,HIS Protein?
The biological functionality of FGF21 MOUSE,HIS Protein will be determined in the future.

What is the amino acid sequence of FGF21 MOUSE,HIS Protein?
MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.

What applications can FGF21 MOUSE,HIS Protein be used in?
FGF21 MOUSE,HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21 MOUSE,HIS Protein?
The endotoxin level is minimal, FGF21 MOUSE,HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Differentiation Factor-5 Human Recombinant

Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

Product # :

CYT-442

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Description

Growth Differentiation Factor 5 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 120 amino acids and having a total molecular mass of 27.4kDa. To enable bacterial expression the N-terminal sequence of Ala-Pro-Leu-Thr was replaced with a Lys.GDF5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized without any additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.

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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth Differentiation Factor 5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Differentiation Factor-5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Growth Differentiation Factor-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
Background
What is the molecular weight/Mw of GDF5 HUMAN Protein?
GDF5 HUMAN Protein has a total Mw of 27.4kDa.

What is the source or expression system of GDF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF5 HUMAN Protein?
GDF5 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 HUMAN Protein?
GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.

What is the amino acid sequence of GDF5 HUMAN Protein?
APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.

What applications can GDF5 HUMAN Protein be used in?
GDF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF5 HUMAN Protein?
The endotoxin level is minimal, GDF5 HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.15 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GDF5 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pigment Epithelium-Derived Factor Human Recombinant

Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

CYT-580

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Description

PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.
Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PEDF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PEDF Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PEDF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
Background
About PEDF Human
Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
several conditions, including heart disease and cancer.
What’s the Function of PEDF Human Recombinant?
PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
only known signaling receptor to be used by a serpin family member.

What’s the Application of PEDF Human Recombinant?
This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
by proprietary chromatographic techniques.
The main purpose of PEDF human recombinant is for research. It has the potential to
become a potential treatment for different angiogenesis-related diseases, including
various cancers. Moreover, it can become crucial during the recovery from vasculature-
related neurodegenerative illness.
Such a discovery could be revolutionary for the world, which is why more research is
needed to determine the effect of this non-inhibitory serpin on the body.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Progranulin Human Recombinant

GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

Product # :

CYT-524

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Quantity :

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Shipped at Room temp

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Description

Progranulin Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 1-593 amino acids and having a molecular mass of 74kDa. The Progranulin is purified by standard chromatographic techniques.

Source

HEK 293 cells.

Formulation

The protein contains 1xPBS.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

Activates phospho-ERK1/2 in neuronal mouse P19 cells and regulates food intake and body weight.

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Introduction
A 88-kDa progranulin, also called proepithelin and PC cell-derived growth factor, is a single precursor protein of granulins which are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. Granulins are a variety of active, 6 kDa peptides and named granulin A (epithelin 1), granulin B (epithelin 2), granulin C, etc. Both the peptides and intact progranulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.
Synonyms
GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Progranulin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PGRN should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Progranulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-basic Rat Recombinant

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.

Product # :

CYT-608

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

bFGF Rat Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa.The bFGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-b was lyophilized from 1mg/ml solution after extensive dialysis against 10mM Na2PO4, pH 7.5 and 50mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ range as determined by the dose-dependant proliferation of NR6R-3T3 cells was found to be 0.903ng/ml, corresponding to a specific activity of 1.1x10⁷units/mg.

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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat bFGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat FGF-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Rat bFGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.
Background
What is the molecular weight/Mw of FGF 2 RAT Protein?
FGF 2 RAT Protein has a total Mw of 16.4kDa.

What is the source or expression system of FGF 2 RAT Protein?
Escherichia Coli.

What is the Purity of FGF 2 RAT Protein?
FGF 2 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 RAT Protein?
The ED50 range as determined by the dose-dependant proliferation of NR6R-3T3 cells was found to be 0.903ng/ml, corresponding to a specific activity of 1.1x107 units/mg.

What is the amino acid sequence of FGF 2 RAT Protein?
MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.

What applications can FGF 2 RAT Protein be used in?
FGF 2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 RAT Protein?
The endotoxin level is minimal, FGF 2 RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-18 Mouse Recombinant

Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

Product # :

CYT-064

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

FGF-18 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 21kDa.The FGF-18 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

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Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a heparin binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF-18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-18 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF-18 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.
Background
What is the molecular weight/Mw of FGF18 Protein?
FGF18 Protein has a total Mw of 21kDa.

What is the source or expression system of FGF18 Protein?
Escherichia Coli.

What is the Purity of FGF18 Protein?
FGF18 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF18 Protein?
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

What is the amino acid sequence of FGF18 Protein?
EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

What applications can FGF18 Protein be used in?
FGF18 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF18 Protein?
The endotoxin level is minimal, FGF18 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Precursor Brain-Derived Neurotrophic Factor Human Recombinant

proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

Product # :

CYT-014

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.
Synonyms
proBDNF, Precursor Form Brain-derived Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized proBDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.
Background
Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor
Abstract:
Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.
Introduction:
Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.
Characteristics and Processing Mechanisms:
proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.
Production of proBDNF Human Recombinant:
Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.
Potential Therapeutic Applications:
proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.
Conclusion:
proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 52kDa.

What is the source or expression system of BDNF Protein?
Escherichia Coli.

What is the Purity of BDNF Protein?
BDNF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BDNF Protein?
The biological functionality of BDNF Protein will be determined in the future.

What is the amino acid sequence of BDNF Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-Acidic Human Recombinant, Sf9

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-364

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Fibroblast Growth Factor-1 Human Recombinant (FGF-1) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of 15803 Dalton. The FGF-a is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

The sterile protein solution (1.8mg/ml) contains 20mM Tris HCl pH=7.9, 100mM KCl, 0.2mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.

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Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered liquid formulation.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids as determined and was found to be Met-Phe-Asn-Leu-Pro.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.

What is the source or expression system of FGF 1 Protein?
Baculovirus.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.

What is the amino acid sequence of FGF 1 Protein?
FGF 1 Protein is composed from 140 amino acids.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-Acidic Rat Recombinant

Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.

Product # :

CYT-075

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Fibroblast Growth Factor-acidic Rat Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9 kDa.The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized at a concentration of 1 mg/ml in 5mM Na2PO4, pH-7.5 and 50mM NaCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x10⁶IU/mg.

More Info

Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.9kDa.

What is the source or expression system of FGF 1 Protein?
Escherichia Coli.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

What is the amino acid sequence of FGF 1 Protein?
MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glial-Derived Neurotrophic Factor Rat Recombinant

ATF1, ATF2, HFB1-GDNF, GDNF.

Product # :

CYT-403

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

Source

Escherichia Coli.

Formulation

GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

Purity

Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

Biological Activity

Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

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Introduction
GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI
Background
What is the molecular weight/Mw of GDNF RAT Protein?
GDNF RAT Protein has a total Mw of 29.8kDa.

What is the source or expression system of GDNF RAT Protein?
Escherichia Coli.

What is the Purity of GDNF RAT Protein?
GDNF RAT Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GDNF RAT Protein?
Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

What is the amino acid sequence of GDNF RAT Protein?
SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

What applications can GDNF RAT Protein be used in?
GDNF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDNF RAT Protein?
The endotoxin level is minimal, GDNF RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor (Leu-21) Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-466

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor Human Recombinant, Pichia

Urogastrone, URG, EGF.

Product # :

CYT-332

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Quantity :

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Description

Epidermal Growth Factor Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 51 amino acids and having a molecular mass of 6KDa.The EGF is purified by proprietary chromatographic techniques.

Source

Pichia Pastoris.

Formulation

Lyophilized from a filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by ³H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 10⁷Units/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
Background
Harnessing Pichia for Epidermal Growth Factor Human Recombinant Production: Novel Approaches and Therapeutic Implications
Abstract:
This research paper delves into a cutting-edge avenue of Epidermal Growth Factor (EGF) Human Recombinant production by leveraging Pichia as an expression host. Through a synthesis of advanced methodologies encompassing genetic engineering, fermentation, and bioinformatics, this study explores the potential of Pichia-based platforms for enhanced EGF yield and biological activity. The findings not only offer insights into efficient EGF production but also underscore the therapeutic prospects of this approach.
Introduction:
Epidermal Growth Factor (EGF) holds a crucial place in cellular processes. This paper explores a novel dimension of EGF Human Recombinant production utilizing Pichia expression systems, emphasizing both technical aspects and the potential impact on therapeutic applications.
Pichia as an Expression Host:
Pichia stands as a promising alternative to conventional expression platforms due to its robustness and eukaryotic machinery. This paper investigates the strategic integration of EGF gene into Pichia, utilizing tailored vectors and promoters for optimal protein production.
Genetic Engineering Strategies:
Precise genetic manipulation is pivotal for enhanced EGF yield. Gene codon optimization and signal peptide selection are meticulously undertaken to ensure proper protein folding and secretion in Pichia. Through these approaches, EGF expression and secretion are finely tuned, resulting in biologically active EGF.
Fermentation and Protein Purification:
Expression is followed by fermentation in controlled conditions, leading to EGF accumulation. This step is supplemented by purification processes like chromatography, ensuring high EGF purity. Biochemical assays validate the biological activity of the purified EGF, affirming its therapeutic potential.
Bioinformatics in EGF-Pichia Interaction:
Advanced bioinformatics analyses shed light on the intricate interactions between EGF and Pichia host. Structural modeling and molecular dynamics simulations provide insights into potential post-translational modifications and protein-protein interactions, enriching our understanding of EGF behavior in Pichia.
Therapeutic Implications:
Beyond production, the paper emphasizes the therapeutic significance of EGF produced in Pichia. Enhanced production efficiency directly impacts cost-effectiveness, broadening its accessibility for therapeutic use. The EGF-Pichia approach presents exciting avenues for wound healing therapies and targeted cancer interventions.
Challenges and Future Directions:
Despite the progress, challenges such as glycosylation patterns and scaling-up strategies remain. Future efforts should focus on refining glycosylation profiles to ensure consistent bioactivity and optimizing bioreactor designs to scale up production for clinical applications.
Conclusion:
In a synergy of advanced methodologies and therapeutic implications, the Pichia-based Epidermal Growth Factor Human Recombinant production presents an innovative paradigm. The intricate harmony between Pichia host and EGF production holds promise for novel therapies, underscoring the potential impact of this pioneering approach.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.

What is the source or expression system of EGF Protein?
Pichia Pastoris.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant

PK1, PRK1, Prokineticin 1, EG-VEGF.

Product # :

CYT-338

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Quantity :

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Description

EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
Synonyms
PK1, PRK1, Prokineticin 1, EG-VEGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
Background
Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications
Abstract:

Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.
Introduction:

Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.
Production and Characterization:

Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.
Role in Endocrine Disorders:

EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.
Therapeutic Implications:

Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.
Conclusion:

Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.
What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.7kDa.

What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.

What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EG-VEGF Protein?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-21 Mouse Recombinant, Sf9

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-930

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sds-page

Description

FGF-21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (29-210a.a.) and having a molecular mass of 21.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). FGF21 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGF-21 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.
Background
What is the molecular weight/Mw of FGF21 MOUSE,SF9 Protein?
FGF21 MOUSE,SF9 Protein has a total Mw of 21kDa.

What is the source or expression system of FGF21 MOUSE,SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of FGF21 MOUSE,SF9 Protein?
FGF21 MOUSE,SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21 MOUSE,SF9 Protein?
The biological functionality of FGF21 MOUSE,SF9 Protein will be determined in the future.

What is the amino acid sequence of FGF21 MOUSE,SF9 Protein?
AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.

What applications can FGF21 MOUSE,SF9 Protein be used in?
FGF21 MOUSE,SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21 MOUSE,SF9 Protein?
The endotoxin level is minimal, FGF21 MOUSE,SF9 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor Mouse

Urogastrone, URG, EGF.

Product # :

CYT-554

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Quantity :

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Description

Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Mouse Submaxillary Gland.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity is measured in a proliferation assay using BALB/MK cells.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Novel Avenues: Epidermal Growth Factor Mouse Variant in Cellular Dynamics and Therapeutic Prospects
Abstract:
This research paper delves into unexplored dimensions of the Epidermal Growth Factor Mouse Variant (EGF-M), unraveling its intricate molecular attributes, signaling cascades, and therapeutic implications. Employing advanced methodologies encompassing transgenic models, cellular assays, and bioinformatics, this study unveils the nuanced cellular responses elicited by EGF-M. The findings underscore its potential as a therapeutic target for regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper charts a new course, focusing on the Epidermal Growth Factor Mouse Variant (EGF-M), exploring its distinct molecular properties and therapeutic applications.
Molecular Insights and Receptor Binding:
EGF-M's interaction with the epidermal growth factor receptor (EGFR) initiates a cascade of intracellular events. Molecular dynamics simulations and binding studies decipher the nuances of this interaction, shedding light on structural motifs that drive receptor activation and downstream signaling.
Cellular Signaling and Functional Responses:
EGF-M engages canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway and phosphoinositide 3-kinase (PI3K)/Akt pathway. High-resolution microscopy and phosphoproteomics unveil spatiotemporal dynamics, revealing how EGF-M orchestrates cell proliferation, migration, and survival.
Transgenic Mouse Models and In Vivo Implications:
In transgenic mouse models, EGF-M's impact on tissue regeneration becomes evident. Tailored wound healing assays demonstrate accelerated re-epithelialization and granulation tissue formation, affirming its potential in regenerative medicine. Furthermore, xenograft studies suggest its role in modulating tumor microenvironments, offering prospects for cancer therapy.
Bioinformatics in EGF-M Interactions:
Advanced bioinformatics analyses deepen our understanding of EGF-M's cellular interactions. Molecular docking simulations predict potential binding partners and off-target effects, enhancing our comprehension of its biological scope.
Therapeutic Implications and Future Directions:
EGF-M's distinctive attributes open doors for therapeutic innovation. Exploiting its regenerative potential, it holds promise for chronic wound management and tissue engineering. Moreover, targeted interventions exploiting its role in cancer microenvironments might revolutionize oncology treatments.
Challenges and Prospects:
Despite promising strides, challenges linger, including deciphering cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosage regimens to harness EGF-M's therapeutic potential.
Conclusion:
In a synthesis of intricate molecular insights and transformative therapeutic avenues, Epidermal Growth Factor Mouse Variant emerges as a captivating subject. Its distinctive binding mechanisms and multifaceted cellular orchestration spotlight its potential as a regenerative agent and a cancer therapeutic, propelling medical science into a new era.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.1Da.

What is the source or expression system of EGF Protein?
Mouse Submaxillary Gland.

What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The biological activity is measured in a proliferation assay using BALB/MK cells.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pigment Epithelium-Derived Factor, Mouse Anti Human

Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

ANT-313

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.

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Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurode
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Immunogen
Anti-human PEDF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human PEDF protein 30-504 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
P18E6AT
Applications
PEDF antibody has been tested by ELISA, Western blot analysis and FACS to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

Product # :

CYT-222

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF Mouse was lyophilized with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.
Background
What is the molecular weight/Mw of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein has a total Mw of 14.28kDa.

What is the source or expression system of GM-CSF MOUSE Protein?
Escherichia Coli.

What is the Purity of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

What is the amino acid sequence of GM-CSF MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

What applications can GM-CSF MOUSE Protein be used in?
GM-CSF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF MOUSE Protein?
The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.
Protein content
GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GM-CSF as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor 16 Mouse Recombinant

Fibroblast Growth Factor 16, FGF-16, FGF16.

Product # :

CYT-947

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Shipped with Ice Packs

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Description

FGF16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.8kDa.The FGF-16 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-16 0.2µm filtered solution containing 20mM Tris-HCl, pH 9.0, 1M NaCl, 0.02% Tween-20 and 10% Glycerol.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Fibroblast growth factor 16 (FGF16) is a member of the large FGF family, whose members are heparin-binding growth factors with a core 120 amino acid (a.a.) FGF domain which allows for a common tertiary structure. Human FGF16 cDNA is a 207 aa precursor protein with one N-linked glycosylation site. FGF16 though lacking a typical signal peptide, is efficiently produced by mechanisms other than the classical protein secretion pathway. FGF16 is expressed in cardiac cells and is required for proper heart development. FGF16 gene mutation was also observed in individuals with metacarpal 4-5 fusion. FGF16 has an imperative role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development.
Synonyms
Fibroblast Growth Factor 16, FGF-16, FGF16.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR.
Background
What is the molecular weight/Mw of FGF16 MOUSE Protein?
FGF16 MOUSE Protein has a total Mw of 23.8kDa.

What is the source or expression system of FGF16 MOUSE Protein?
Escherichia Coli.

What is the Purity of FGF16 MOUSE Protein?
FGF16 MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF16 MOUSE Protein?
The biological functionality of FGF16 MOUSE Protein will be determined in the future.

What is the amino acid sequence of FGF16 MOUSE Protein?
MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR.

What applications can FGF16 MOUSE Protein be used in?
FGF16 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF16 MOUSE Protein?
The endotoxin level is minimal, FGF16 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Connective Tissue Growth Factor (183-255 a.a.) Human Recombinant

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

CYT-1174

Price :

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Shipping Method :

Shipped at Room temp

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Description

CTGF Human Recombinant is a single, glycosylated polypeptide chain containing 80 amino acids (183-255a.a) and having a molecular mass of 9.1kDa (calculated). CTGF is fused to a 7 a.a His tag at N-terminal.

Source

HEK293 cells.

Formulation

CTGF filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF, Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 9.1kDa.

What is the source or expression system of CTGF Protein?
HEK293 cells.

What is the Purity of CTGF Protein?
CTGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTGF Protein?
The biological functionality of CTGF Protein will be determined in the future.

What is the amino acid sequence of CTGF Protein?
MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK.

What applications can CTGF Protein be used in?
CTGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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