Search: 1000 results found for "hdgf"

Description:

Glia Maturation Factor Beta Human His Tag Recombinant

GMF, GMF beta.

Product # :

CYT-726

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Description

GMFB Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 162 amino acids (1-142 a.a.)and having a total molecular mass of 18.8 kDa. GMGB is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMFB 1mg/ml protein solution contains 20mM Tris-HCL pH-8, 1mM DTT, 0.1M NaCl and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
Synonyms
GMF, GMF beta.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSESLVVCDV AEDLVEKLRK FRFRKETNNA AIIMKIDKDK RLVVLDEELE GISPDELKDE LPERQPRFIV
YSYKYQHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNK LVQTAELTKV FEIRNTEDLT EEWLREKLGF FH.
Background
What is the molecular weight/Mw of GMFB HIS HUMAN Protein?
GMFB HIS HUMAN Protein has a total Mw of 18.8kDa.

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

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

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

What is the amino acid sequence of GMFB HIS HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MSESLVVCDV AEDLVEKLRK FRFRKETNNA AIIMKIDKDK RLVVLDEELE GISPDELKDE LPERQPRFIV
YSYKYQHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNK LVQTAELTKV FEIRNTEDLT EEWLREKLGF FH.

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

What is the endotoxin level for GMFB HIS HUMAN Protein?
The endotoxin level is minimal, GMFB HIS 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:

Platelet-Derived Growth Factor Receptor, Alpha Human Recombinant

Platelet-derived growth factor receptor alpha polypeptide, PDGFR2, PDGF-R-alpha, CD140 antigen-like family member A, CD140a antigen, alpha-type platelet-derived growth factor receptor, RHEPDGFRA, rearranged-in-hypereosinophilia-platelet derived growth factor receptor alpha, PDGFRA/BCR fusion protein, MGC74795, EC 2.7.10.1.

Product # :

CYT-065

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Description

PDGFRA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 522 amino acids (24-524) and having a molecular mass of 58.4 kDa.The PDGFRA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PDGFRA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
PDGFRa is a cell surface tyrosine kinase receptor for PDGF family members. PDGFRa binds to both A and B subunits of PDGF. It is known that PDGFRa is vital for kidney development since mice heterozygous for the receptor display defective kidney phenotypes.
Synonyms
Platelet-derived growth factor receptor alpha polypeptide, PDGFR2, PDGF-R-alpha, CD140 antigen-like family member A, CD140a antigen, alpha-type platelet-derived growth factor receptor, RHEPDGFRA, rearranged-in-hypereosinophilia-platelet derived growth factor receptor alpha, PDGFRA/BCR fusion protein, MGC74795, EC 2.7.10.1.
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 MQLSLPSILP NENEKVVQLN SSFSLRCFGE SEVSWQYPMS EEESSDVEIR NEENNSGLFV TVLEVSSASA AHTGLYTCYY NHTQTEENEL EGRHIYIYVP DPDVAFVPLG MTDYLVIVED DDSAIIPCRT TDPETPVTLH NSEGVVPASY DSRQGFNGTF TVGPYICEAT VKGKKFQTIP FNVYALKATS ELDLEMEALK TVYKSGETIV VTCAVFNNEV VDLQWTYPGE VKGKGITMLE EIKVPSIKLV YTLTVPEATV KDSGDYECAA RQATREVKEM KKVTISVHEK GFIEIKPTFS QLEAVNLHEV KHFVVEVRAY PPPRISWLKN NLTLIENLTE ITTDVEKIQE IRYRSKLKLI RAKEEDSGHY TIVAQNEDAV KSYTFELLTQ VPSSILDLVD DHHGSTGGQT VRCTAEGTPL PDIEWMICKD IKKCNNETSW TILANNVSNI ITEIHSRDRS TVEGRVTFAK VEETIAVRCL AKNLLGAENR ELKLVAPTLR SE.

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 1 Human Recombinant, HEK

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

Product # :

CYT-1260

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Description

TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.

Source

HEK 293 cells.

Formulation

Lyophilized from a sterile filtered solution containing TFA (0.1%).

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 10⁷ units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 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 TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are 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.

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 Human Recombinant , HEK

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

Product # :

CYT-687

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Description

The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues (aa 27-349) including a C-terminal 6×His tag.

Source

HEK293 cells.

Formulation

CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7 and 20% (w/v) glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
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: fibrosis, vascular ailments and tumorigenesis.
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 four 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. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
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.
Physical Appearance
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
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 36kDa.

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

What is the Purity of CTGF Protein?
CTGF Protein is >90% 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?
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

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.

Description:

beta Nerve Growth Factor Human Recombinant, HEK

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-079

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Description

BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.

Source

HEK293 cells.

Formulation

The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.

Purity

Greater than 97% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED₅₀ is <0.04-0.4ng/ml.

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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF 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 b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.

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

What is the Purity of B NGF Protein?
B NGF Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of B NGF Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.

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

What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF 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:

Gametocyte Specific Factor 1 Human Recombinant

Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

Product # :

PRO-561

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Description

GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
Physical Appearance
Sterile Filtered 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
MGSSHHHHHH SSGLVPRGSH MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.

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:

Platelet-derived Growth Factor AA Human Recombinant, Yeast

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

Product # :

CYT-568

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Description

PDGF-AA Human Recombinant produced in Yeast is a homodimeric, glycosilated, polypeptide chain containing 2 x 110 amino acids and having a total molecular mass of 34 kDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Pichia Pastoris.

Formulation

The protein was lyophilized with 20mM sodium phosphate buffer.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was found to be 1ng/ml corresponding to a Specific Activity of 1,000,000IU/mg calculated by the ability to stimulate the proliferation of mouse 3T3 fibroblasts (PNAS 94, 10205, 1997. Biochemistry, 1996, 35, 12077).

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PDGF-AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 PDGF-AA 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:

Growth Differentiation Factor-3 Human Recombinant

Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

Product # :

CYT-694

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Description

GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.
Synonyms
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
Background
What is the molecular weight/Mw of GDF3 HUMAN Protein?
GDF3 HUMAN Protein has a total Mw of 14.15XkDa.

What is the source or expression system of GDF3 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF3 HUMAN Protein?
GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF3 HUMAN Protein?
The biological functionality of GDF3 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF3 HUMAN Protein?
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

What applications can GDF3 HUMAN Protein be used in?
GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF3 HUMAN Protein?
The endotoxin level is minimal, GDF3 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:

Placental Growth Factor-2, HEK Human Recombinant

PIGF, PGF, PlGF-2, PLGF-2.

Product # :

CYT-1228

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Description

PLGF2 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-170) containing 158 amino acids and having a molecular mass of 18.1kDa. PLGF2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

PLGF2 protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human VEGFR1/Flt-1.

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Synonyms
PIGF, PGF, PlGF-2, PLGF-2.
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
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RRHHHHHH.
Background
PLGF2, a homodimeric glycoprotein, exhibits a unique structural configuration essential for its interactions with VEGF receptors and other signaling molecules. The human recombinant form provides a controlled platform for studying the three-dimensional structure of PLGF2, elucidating its binding affinities and conformational dynamics. Understanding its structure is fundamental for deciphering how PLGF2 mediates angiogenic signaling and vascular remodeling.

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:

Platelet-derived Growth Factor AA Mouse Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

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CYT-590

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Description

PDGF-AA Mouse Recombinant is a disulfide linked homodimeric, non-glycosylated, polypeptide chain containing 2 x 126 amino acids and having a total molecular mass of 28.9 kDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Established by the dose-dependent stimulation of Balb/c 3T3 cells proliferation. The expected ED50 for this effect is 8-10 ng/ml corresponding to a specific activity of 100,000-125,000IU/mg.

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PDGF-AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 PDGF-AA in sterile 18MΩ-cm H2O at a concentration ranging between 0.1-0.5mg per 1ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSIEEAVPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATSNLN PDHREEETGR RRESGKNRKR KRLKPT.

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-Alpha Human Recombinant

Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.

Product # :

CYT-871

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Description

TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 0.1% TFA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.

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Introduction
Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.
Synonyms
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFA 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 TGFA in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.
Background
Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications
Abstract:

Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.
Introduction:

TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.
Production Process and Characteristics:

TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.
Therapeutic Applications:

TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.
Advantages and Challenges:

The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.
Conclusion:

TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.

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:

GH Mouse Recombinant

GH1, GH, GHN, GH-N, hGH-N, Pituitary GH, GH-1.

Product # :

CYT-540

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Description

Growth Hormone Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids and having a molecular mass of 22 kDa. Mouse GH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Mouse Growth Hormone Recombinant Lyophilized from a 0.2 μm filtered solution of 20mM HEPES, 4% Sucrose, 4% Mannitol, 0.02% Tween 80, pH 8.0.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH 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 GHs, 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 GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary GH, GH-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH mouse 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 Hormone Murine 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:

Platelet-Derived Growth Factor AA Rat Recombinant

Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.

Product # :

CYT-776

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Description

Platelet-derived Growth Factor AA Human Recombinant is a disulfide-linked homodimer Consists of two A chains containing 111 amino acids each and having a total molecular mass of 25.3KDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PDGF-AA was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.0.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 10⁵ IU/mg.

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF
have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-derived Growth Factor AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 Platelet-derived Growth Factor-AA in Sterile 4mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
MSIEEAIPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATSNLN PDHREEETDV R.

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:

Keratinocye Growth Factor Mouse Recombinant

HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.

Product # :

CYT-721

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Description

Keratinocyte Growth Factor-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18.9 kDa. The FGF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Phosphate buffer pH-8 and 0.1M NaCl.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant stimulation of KGF-responsive BaF3 indicator cells (measured by 3H-thymidine uptake) is < 10ng/ml corresponding to a specific activity of 100,000 Units/mg.

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Introduction
KGF 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. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
Synonyms
HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 KGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCNDMSPEQT ATSVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNSYNIMEI RTVAVGIVAI KGVESEYYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHSG GEMFVALNQK GIPVKGKKTK KEQKTAHFLP MAIT.

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 2 Human Recombinant, HEK

Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

Product # :

CYT-112

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Description

TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED₅₀ is 0.16ng/ml.

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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

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 Human Recombinant, HEK

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

Product # :

CYT-113

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Description

TGF-beta 3 Human Recombinant produced in HEK cells is a homodimer containing 2 x 112 amino acids linked by a disulfide bond having a total molecular weight of 25kDa. The TGF-b 3 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The TGF-b 3 was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2) and is typically 0.05 ng/ml corresponding to a specific activity of ≥ 20,000,000 units/mg.

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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 White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGF-b 3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 3 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 TGF-b 3 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
MALDTNYCFR NLEENCCVRP LYIDFRQDLG WKWVHEPKGY YANFCSGPCP YLRSADTTHS TVLGLYNTLN PEASASPCCV PQDLEPLTIL YYVGRTPKVE QLSNMVVKSC KCS

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:

Platelet-Derived Growth Factor BB Mouse Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

Product # :

CYT-412

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Description

Platelet-Derived Growth Factor BB Mouse Recombinant produced in E.coli, is a homodimeric, non-glycosylated, polypeptide chain containing 2x110 (total of 2 chains 220aa) amino acids and having a total molecular weight of 24.7 kDa.PDGF-BB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 10mM NaCitrate pH-3.0.

Purity

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

Biological Activity

The biological activity is determined by the dose-dependant stimulation of the proliferation of human umbelical vein endothelial cells (HUVEC) using a concentration range of less than 1.6ng/ml.

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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 Platelet-derived Growth Factor-BB in sterile 100mM acetic acid and 0.1% BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSLGSLAAAE PAVIAECKTR TEVFQISRNL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRASQVQMRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETIVTPRPVT
Background
Platelet-Derived Growth Factor BB (PDGF-BB) is one of the isoforms of the PDGF family that plays a significant role in embryonic development, cell proliferation, cell migration, and angiogenesis.
It's also relevant in the context of certain pathologies like cancer or healing processes.
Here's what a research paper on Mouse Recombinant PDGF-BB might involve:
Basic Biology:
It might discuss the basic biology and function of PDGF-BB in the mouse model. This could include its role in various cellular processes like cell growth, division, and survival, as well as in the context of tissue repair or angiogenesis.

Recombinant PDGF-BB Production:
The paper might describe methods for producing recombinant PDGF-BB in laboratory conditions. It might go into detail on the expression system used (e.g., bacterial, yeast, or mammalian cells), the purification process, and how the functionality of the produced PDGF-BB was confirmed.

Applications:
It could also detail the experimental applications of recombinant PDGF-BB in the mouse model. For instance, it could be used to study wound healing processes, tissue regeneration, or the development and progression of certain diseases.
Comparative Analysis:
The research might include a comparison of the recombinant PDGF-BB with its natural counterpart in terms of functionality, structure, or other properties.

Innovation:
If the paper is presenting new research, it might discuss an innovative use of PDGF-BB, a novel production method, or new findings about its function.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.48 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 PDGF-BB 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:

Growth differentiation factor 5 Mouse Recombinant, His Tag

Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

Product # :

CYT-852

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sds-page

Description

GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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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
Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.
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 MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.
Background
What is the molecular weight/Mw of GDF5 MOUSE Protein?
GDF5 MOUSE Protein has a total Mw of 16kDa.

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

What is the Purity of GDF5 MOUSE Protein?
GDF5 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 MOUSE Protein?
The biological functionality of GDF5 MOUSE Protein will be determined in the future.

What is the amino acid sequence of GDF5 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

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

What is the endotoxin level for GDF5 MOUSE Protein?
The endotoxin level is minimal, GDF5 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:

Fibroblast Growth Factor-8 Human Recombinant, HEK

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Product # :

CYT-087

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Description

FGF-8 Human Recombinant is a single, glycosylated, polypeptide chain (23-215 a.a) containing a total of 204 amino acids and having a molecular mass of 23.7 kDa. FGF-8 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The FGF-8 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90% as obsereved by SDS-PAGE.

Biological Activity

The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.

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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
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
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 23.7kDa.

What is the source or expression system of FGF8 Protein?
HEK.

What is the Purity of FGF8 Protein?
FGF8 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.

What is the amino acid sequence of FGF8 Protein?
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.

What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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:

GHBP Human Recombinant

Product # :

CYT-238

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

GHBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids and having a molecular mass of 28107.01 Dalton. GHR is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GHBP was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

GHBP is fully biologically active as evidenced by its ability of forming 2:1 complex with G.H.

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Introduction
GHBP is a transmembrane receptor for GH. Binding of GH to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the GH insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GHBP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP 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 GHBP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AFSGSEATAAILSRAPWSLQSVNPGLKTNS SKEPKFTKCRSPERETFSCHWTDEVHHGTK
NLGPIQLFYTRRNTQEWTQEWKECPDYVSA GENSCYFNSSFTSIWIPYCIKLTSNGGTVD
EKCFSVDEIVQPDPPIALNWTLLNVSLTGI HADIQVRWEAPRNADIQKGWMVLEYELQYK
EVNETKWKMMDPILTTSVPVYSLKVDKEYE VRVRSKQRNSGNYGEFSEVLYVTLPQMSQF
TCEEDFYF.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.6 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 GHBP 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:

Glial-Derived Neurotrophic Factor Human Recombinant, Sf9

Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.

Product # :

CYT-1162

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GDNF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.
Synonyms
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
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
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
Background
What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.

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

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

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

What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH

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

What is the endotoxin level for GDNF HUMAN, SF9 Protein?
The endotoxin level is minimal, GDNF HUMAN, 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:

Growth Hormone Binding Protein Mouse Recombinant

GHR, GHBP, GH receptor, Somatotropin receptor.

Product # :

CYT-1256

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

Growth Hormone Binding Protein Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids and having a molecular mass of 28 kDa. GHBP Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Growth Hormone Binding Protein Mouse was lyophilized from a concentrated (1mg/ml) solution with 0.5mg/ml NaHCO3.

Purity

Greater than 95.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

fully biologically active as evidenced by its ability of forming 2:1 complex with human and non-primate GHs.

More Info

Synonyms
GHR, GHBP, GH receptor, Somatotropin receptor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GHBP Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -20C. Upon reconstitution at > 0.1 GHBP Mouse -ECD mg/ml and filter sterilization GHBP can be stored at 4C for several weeks. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GHBP Mouse in sterile 0.4% NaHCO3 adjusted to pH 8 or in distilled water, 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 Ala-Phe-Ser-Gly-Ser.
Background
GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon 3 and has been well-characterized. Mutations in GHBP have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short height.

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 Human Recombinant

Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-218

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.The FGF-b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.

Purity

Greater than 98.0% as determined by Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x10⁷ Units/mg.

More Info

Introduction
Basic 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 HPR -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
Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fibroblast Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b 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 Fibroblast Growth Factor Basic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.
Background
FGF 2 HUMAN: Insights into Fibroblast Growth Factor-2
Basic Fibroblast Growth Factor or FGF 2 HUMAN is a protein with crucial roles in cell growth, tissue repair, and embryonic development. This is part of the larger fibroblast growth factor family and is vital for various biological processes, including the modulation of cell survival activities.
Production and Properties
Produced in E. coli, FGF 2 is a non-glycosylated polypeptide chain possessing 154 amino acids with a molecular weight of about 17.2 kDa. It is purified through advanced chromatographic techniques, ensuring high purity and activity for laboratory use.
Physical Characteristics and Preparation
The physical form of FGF 2 HUMAN is a sterile, white lyophilized powder. For experimental use, it is reconstituted with sterile water to at least 100µg/ml. This reconstitution is crucial for maintaining the integrity and effectiveness of the protein in various research applications.
Storage and Handling
To maintain stability, lyophilized FGF 2 should be stored at -18°C and used within three weeks if kept at room temperature. Once reconstituted, it should be kept at 4°C and used within 2-7 days or stored at -18°C for longer-term storage.
Proper handling and avoiding repeated freeze-thaw cycles are essential to preserve the protein's functionality.
Purity and Biological Activity
FGF 2 is characterized by a purity greater than 98%, verified by SDS-PAGE analysis. Its biological activity is primarily defined by its efficacy in promoting the proliferation of specific cell lines, with an effective dose (ED50) typically below 0.1 ng/ml.
Research Applications and Impact
In the research context, FGF 2 is used extensively to study its effects on cell migration, proliferation, and angiogenesis. Moreover, its role in disease models, particularly in cancer and tissue repair studies, makes it a valuable resource for developing new therapeutic approaches.
Usage Guidelines
FGF 2 HUMAN is strictly for laboratory research use and is not suitable for drug development, food production, or cosmetic applications. Researchers are advised to comply with safety and handling guidelines to ensure that experiments are conducted under optimal conditions.
The Broad Impact on Development and Disease
FGF-2 is known for its multifunctional role across numerous biological processes such as tissue repair, embryonic development, angiogenesis, and even tumorigenesis.
This growth factor, existing in various synonymous forms such as Basic FGF, FGF-b, and HBGF-2, is essential in cellular processes that underpin both health and disease.
Furthermore, FGF-2's ability to bind to cellular receptors triggers a cascade of signaling pathways, including PI3K/Akt, MAPK/ERK, and PLCγ, which in turn influence cell growth, migration, and survival.
These pathways are pivotal in mediating the factor's diverse effects on cell behavior, contributing to its critical roles in wound healing, angiogenesis, and tissue remodeling.
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.2kDa.

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

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

What is the amino acid sequence of FGF 2 Protein?
AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

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

What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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 and Differentiation Factor 15 Human Recombinant, His Tag

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-691

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

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 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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

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

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

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

What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

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

What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, 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.

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