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Description:

Growth and Differentiation factor 5 Mouse Recombinant

Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5, Growth/differentiation factor 5.

Product # :

CYT-941

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Description

GDF5 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.2kDa.The GDF-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF-5 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000IU/mg.

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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, Growth/differentiation factor 5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-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 GDF5 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
Background
What is the molecular weight/Mw of GDF5 MOUSE Protein?
GDF5 MOUSE Protein has a total Mw of 27.2kDa.

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 >96% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 MOUSE Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000IU/mg.

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

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-5 Human Recombinant

Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.

Product # :

CYT-957

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Description

FGF5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 252 amino acids and having a molecular mass of 27.7kDa.The FGF-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-5 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 100mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor-5 (FGF5) belongs to the FGF family of mitogenic peptides. In vitro, rhFGF5 is a mitogen for Balb/3T3 fibroblasts and bovine heart endothelial cells. FGF5 is also a major muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF5 is assumed to play central roles in both embryology and neurobiology. Developmentally, FGF5 mRNA is originally found in the embryoblast followed by the lateral somatic mesoderm, where it may play a part in angiogenesis, as well as the myotomes cranial to the tail region, where it may delay terminal myoblast differentiation during cell migration.
Synonyms
Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-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 FGF5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
Background
What is the molecular weight/Mw of FGF5 HUMAN Protein?
FGF5 HUMAN Protein has a total Mw of 27.7kDa.

What is the source or expression system of FGF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF5 HUMAN Protein?
FGF5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF5 HUMAN Protein?
The biological functionality of FGF5 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FGF5 HUMAN Protein?
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
What applications can FGF5 HUMAN Protein be used in?
FGF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF5 HUMAN Protein?
The endotoxin level is minimal, FGF5 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:

Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9

Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.

Product # :

PRO-2219

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Description

SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
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
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK HHHHHH.

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-3 Human Recombinant

Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

Product # :

CYT-969

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Description

PLGF3 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x204 amino acids and having a total molecular mass of 45.8kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
Synonyms
Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-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 PLGF-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLPAVPPQQW ALSAGNGSSE VEVVPFQEVW GRSYCRALER LVDVVSEYPS EVEHMFSPSC VSLLRCTGCC GDENLHCVPV ETANVTMQLL KIRSGDRPSY VELTFSQHVR CECRHSPGRQ SPDMPGDFRA DAPSFLPPRR SLPMLFRMEW GCALTGSQSA VWPSSPVPEE IPRMHPGRNG KKQQRKPLRE KMKPERCGDA VPRR.

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 Bovine Recombinant

Fibroblast growth factor 21, FGF-21, FGF21.

Product # :

CYT-657

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Description

Fibroblast Growth Factor -21 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids, having a molecular weight of 19.5 kDa.The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.8 mg/ml) solution with 0.4 mg/ml of NaHCO3, pH 8.

Purity

Greater than 98.0% as determined by:
(a) Analysis by Gel Filtration.
(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 desensitization and to improve, 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, FGF21.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized FGF-21 Bovine 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 reconstitute the lyophilized Bovine FGF-21 in sterile water or 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-His-Pro-Ile-Pro.
Background
What is the molecular weight/Mw of FGF 21 BOVINE Protein?
FGF 21 BOVINE Protein has a total Mw of 19.5kDa.

What is the source or expression system of FGF 21 BOVINE Protein?
Escherichia Coli.

What is the Purity of FGF 21 BOVINE Protein?
FGF 21 BOVINE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 21 BOVINE Protein?
The biological functionality of FGF 21 BOVINE Protein will be determined in the future.

What is the amino acid sequence of FGF 21 BOVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-His-Pro-Ile-Pro.

What applications can FGF 21 BOVINE Protein be used in?
FGF 21 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 21 BOVINE Protein?
The endotoxin level is minimal, FGF 21 BOVINE Protein was purified using conventional chromatography techniques.
Protein content
Bovine FGF-21 quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.47 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 FGF-21 Recombinant 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:

Placental Growth Factor-2 Human Recombinant

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

Product # :

CYT-1116

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Description

Placental Growth Factor-2 Human Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked homodimer consisting of 2x152 amino acid polypeptide chains, having a total molecular mass of approximately 34.6kDa. PLGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

Purity

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

Biological Activity

Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-50 ng/ml.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
PLGF-2 binds neuropilin-1 and 2 in a dependent way.
Synonyms
PIGF, PGF, PlGF-2, PLGF-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PLGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Growth Factor-2 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 Placental Growth Factor-2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RR.

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 (24-412 a.a.) Human Recombinant

Transforming Growth Factor, Beta 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.

Product # :

CYT-886

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Description

TGFB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (24-412 a.a) and having a molecular mass of 47.2kDa. TGFB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGFB3 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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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, Beta 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.
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 MGSLSTCTTL DFGHIKKKRV EAIRGQILSK LRLTSPPEPT VMTHVPYQVL ALYNSTRELL EEMHGEREEG CTQENTESEY YAKEIHKFDM IQGLAEHNEL AVCPKGITSK VFRFNVSSVE KNRTNLFRAE FRVLRVPNPS SKRNEQRIEL FQILRPDEHI AKQRYIGGKN LPTRGTAEWL SFDVTDTVRE WLLRRESNLG LEISIHCPCH TFQPNGDILE NIHEVMEIKF KGVDNEDDHG RGDLGRLKKQ KDHHNPHLIL MMIPPHRLDN PGQGGQRKKR ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

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 (113 a.a.) Human Recombinant

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

Product # :

CYT-679

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Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 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 beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.
Introduction:

TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.
Production Process and Characteristics:

TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.
Therapeutic Applications:

TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.
Advantages and Challenges:

The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.
Conclusion:

TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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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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:

Insulin-Like Growth Factor 1 Des (1-3) Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).

Product # :

CYT-518

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Description

IGF-I Des(1-3) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids (aa 4-70) and having a molecular mass of 7368.5 Dalton. IGF-1 Des1-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.

Purity

Greater than 97% 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 FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×10⁵ units/mg.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF-I des(1-3) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 des-1-3 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 IGF-I des(1-3) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.
Background
What is the molecular weight/Mw of IGF1 HUMAN DES1-3 Protein?
IGF1 HUMAN DES1-3 Protein has a total Mw of 7.3kDa.

What is the source or expression system of IGF1 HUMAN DES1-3 Protein?
Escherichia Coli.

What is the Purity of IGF1 HUMAN DES1-3 Protein?
IGF1 HUMAN DES1-3 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 HUMAN DES1-3 Protein?
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×105 units/mg.

What is the amino acid sequence of IGF1 HUMAN DES1-3 Protein?
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.

What applications can IGF1 HUMAN DES1-3 Protein be used in?
IGF1 HUMAN DES1-3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 HUMAN DES1-3 Protein?
The endotoxin level is minimal, IGF1 HUMAN DES1-3 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 14 Human Recombinant

Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.

Product # :

CYT-756

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Description

FGF14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-247 a.a) and having a molecular mass of 30kDa.FGF14 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

FGF14 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Fibroblast Growth Factor 14 (FGF14) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in a various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF14 gene mutation is linked with autosomal dominant cerebral ataxia.
Synonyms
Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.
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
MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.
Background
What is the molecular weight/Mw of FGF14 Protein?
FGF14 Protein has a total Mw of 30kDa.

What is the source or expression system of FGF14 Protein?
Escherichia Coli.

What is the Purity of FGF14 Protein?
FGF14 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF14 Protein?
The biological functionality of FGF14 Protein will be determined in the future.

What is the amino acid sequence of FGF14 Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.

What applications can FGF14 Protein be used in?
FGF14 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF14 Protein?
The endotoxin level is minimal, FGF14 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:

Fibroblast Growth Factor Receptor 4 Fc Chimera Human Recombinant

Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

Product # :

PKA-233

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Description

Soluble FGFR-4a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain and having a molecular mass of 170 kDa. The FGFR4 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

CD334 was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells. The ED50 for this effect is typically at 15.0-30.0 ng/ml.

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Introduction
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGFR4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFR4 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 FGFR-4 in sterile PBS not less than 100 µg/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-8 Mouse Recombinant, 194 a.a.

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

Product # :

CYT-840

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Description

FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

Biological Activity

The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

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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 White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 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 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 22.5kDa.

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

What is the Purity of FGF8 Protein?
FGF8 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

What is the amino acid sequence of FGF8 Protein?
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

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:

Transforming Growth Factor-beta 1 Human

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

Product # :

CYT-561

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Description

Human Transforming Growth Factor-beta 1 purified from Human Platelets having a molecular mass of 25kDa.The TGF-b 1 is purified by proprietary chromatographic techniques.

Source

Human Platelets.

Formulation

TGF-Beta1 protein was lyophilized from a solution containing 30% acetonitrile and 0.1% trifluoroacetic acid.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

Stimulates the growth of NRK-1 cells in soft agar at concentrations ranging from 0.1 to 5ng/ml corresponding to a specific activity of 200,000-10,000,000IU/mg. Effective concentration ranges must be experimentally determined. Purified EGF and/or TGF- must be present for observation of the biological activity.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 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 beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
Physical Appearance
Sterile Filtered lyophilized powder.
Stability
Lyophilized TGF-beta 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C.DO NOT RECONSTITE WITH NEUTRAL BUFFERS.DO NOT USE GLASS IMPLEMENTS OR EXTENSIVE MANIPULATIONS.PREVENT FREEZE THAW CYCLES.
Solubility
It is recommended to reconstitute lyophilized TGF-beta 1 in 0.5% BSA in 0.1N acetic acid, which can then be further diluted to the desired aliquot with 30% acetonitrile and 0.1% trifluoroacetic acid.
Background
Title: Transforming Growth Factor-Beta 1 Human: An Insight into its Role in Cellular Regulation
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a critical role in various cellular processes, including cell growth, differentiation, apoptosis, and immune regulation. This research paper aims to provide a comprehensive overview of the structure, synthesis, signaling pathways, and biological functions of TGF-β1 in human cells. Additionally, this article highlights the relevance of TGF-β1 in various physiological and pathological conditions, including cancer, fibrosis, and immune disorders. Furthermore, potential therapeutic strategies targeting TGF-β1 signaling are also discussed. The information presented in this paper consolidates the current understanding of TGF-β1 and its significance in cellular regulation.
Introduction:

Transforming Growth Factor-Beta 1 (TGF-β1) belongs to a superfamily of growth factors that regulate various cellular processes. It is synthesized as a precursor protein and undergoes proteolytic cleavage to generate the biologically active form. TGF-β1 exerts its effects by binding to specific cell surface receptors, leading to the activation of downstream signaling cascades. These signaling pathways involve Smad-dependent and Smad-independent mechanisms, which ultimately regulate gene expression and cellular responses.
Biological Functions:

TGF-β1 regulates cell proliferation by exerting both stimulatory and inhibitory effects, depending on the cellular context. It plays a crucial role in tissue development, wound healing, and tissue repair by promoting extracellular matrix synthesis and modulating the immune response. TGF-β1 also has immunomodulatory functions, influencing the differentiation and function of immune cells. However, dysregulation of TGF-β1 signaling is associated with various pathologies, including cancer progression, fibrosis, and autoimmune disorders.
Role in Cancer:

TGF-β1 acts as a tumor suppressor in early stages of cancer by inhibiting cell proliferation and inducing apoptosis. However, in advanced stages, it promotes tumor progression by enhancing tumor cell migration, invasion, and angiogenesis. The dual role of TGF-β1 in cancer highlights its complex involvement in tumorigenesis.
Therapeutic Implications:

Given the significant role of TGF-β1 in various diseases, targeting its signaling pathways has emerged as a potential therapeutic strategy. Several approaches, including small molecule inhibitors, antibodies, and gene therapies, are being explored to modulate TGF-β1 activity in a controlled manner. These interventions hold promise in the treatment of cancer, fibrosis, and other TGF-β1-related disorders.
Conclusion:

Transforming Growth Factor-Beta 1 is a versatile cytokine with diverse functions in cellular regulation. Its role in physiological processes and disease pathogenesis underscores its importance as a therapeutic target. Further investigations into the precise mechanisms and downstream effects of TGF-β1 signaling will contribute to the development of novel therapies for various human disorders.

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

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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:

Fibroblast Growth Factor-4 Human Recombinant

HBGF4, FGF-4, FGF4, KFGF, HSTF1.

Product # :

CYT-312

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Shipped at Room temp

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Description

FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X10⁶ units/mg.

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Introduction
FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.
Synonyms
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 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 FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
Background
What is the molecular weight/Mw of FGF4 HUMAN Protein?
FGF4 HUMAN Protein has a total Mw of 19.8kDa.

What is the source or expression system of FGF4 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF4 HUMAN Protein?
FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF4 HUMAN Protein?
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

What is the amino acid sequence of FGF4 HUMAN Protein?
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

What applications can FGF4 HUMAN Protein be used in?
FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF4 HUMAN Protein?
The endotoxin level is minimal, FGF4 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:

Fibroblast Growth Factor-Acidic Human Recombinant

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

Product # :

CYT-264

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Description

Fibroblast Growth Factor-acidic Human Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 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, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/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 hep-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 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 at 4 degrees Celsius at a concentration of 0.1mg-0.25mg per 1ml. Allow sample to sit for 5 min. at 4 degrees, spin to remove precipitant.
Amino Acid Sequence
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.

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 >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 mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.

What is the amino acid sequence of FGF 1 Protein?
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS 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:

Fibroblast Growth Factor-Basic Bovine Recombinant

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.

Product # :

CYT-288

Price :

Quantity :

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Shipped at Room temp

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Description

FGF-2 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17250 Dalton. The Fibroblast Growth Factor 2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF-b Bovine was lyophilized from a concentrated (1mg/ml) sterile solution containing 1% HSA.

Purity

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

Biological Activity

The ED₅₀, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be <0.1ng/ml, corresponding to a specific activity of 3 x 10⁶Units/mg.

More Info

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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fibroblast Growth Factor 2 Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b Bovine Recombinant 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-2 Bovine Recombinant 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 Met-Ala-Ala-Gly-Ser.
Background
What is the molecular weight/Mw of FGF-2 BOVINE Protein?
FGF-2 BOVINE Protein has a total Mw of 17.5kDa.

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

What is the Purity of FGF-2 BOVINE Protein?
FGF-2 BOVINE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF-2 BOVINE Protein?
The ED50, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be <0.1ng/ml, corresponding to a specific activity of 3 x 106 Units/mg.

What is the amino acid sequence of FGF-2 BOVINE Protein?
FGF-2 BOVINE Protein is composed from 155 amino acids.

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

What is the endotoxin level for FGF-2 BOVINE Protein?
The endotoxin level is minimal, FGF-2 BOVINE 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 0.85 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 FGF-2 Bovine 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 Receptor-4 Human Recombinant, His Tag

Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

Product # :

PKA-090

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Quantity :

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Shipped with Ice Packs

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Description

Fibroblast Growth Factor Receptor-4 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (22-369a.a.) and having a molecular mass of 39.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).FGFR4 is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGFR4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
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
LEASEEVELE PCLAPSLEQQ EQELTVALGQ PVRLCCGRAE RGGHWYKEGS RLAPAGRVRG WRGRLEIASF LPEDAGRYLC LARGSMIVLQ NLTLITGDSL TSSNDDEDPK SHRDPSNRHS YPQQAPYWTH PQRMEKKLHA VPAGNTVKFR CPAAGNPTPT IRWLKDGQAF HGENRIGGIR LRHQHWSLVM ESVVPSDRGT YTCLVENAVG SIRYNYLLDV LERSPHRPIL QAGLPANTTA VVGSDVELLC KVYSDAQPHI QWLKHIVING SSFGADGFPY VQVLKTADIN SSEVEVLYLR NVSAEDAGEY TCLAGNSIGL SYQSAWLTVL PEEDPTWTAA APEARYTDLE HHHHHH.

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:

Macrophage Colony Stimulating Factor Human Recombinant, Baculovirus

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.

Product # :

CYT-637

Price :

Quantity :

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Shipped at Room temp

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Description

Macrophage Colony Stimulating Factor Human Recombinant produced in Baculovirus is a disulfide linked homodimer, glycosylated, polypeptide chain containing 2 x 149 amino acids and having a total molecular mass of 42 kDa.MCSF is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Silkworm.

Formulation

The lyophilized protein (1mg/ml) was lyophilized with 20mM phosphate buffer, 1% HSA and 3% manntiol.

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 stimulation of the proliferation of murine M-NFS-60 indicator cells was found < 3ng/ml, corresponding to a specific activity of less than 333,333.33units/mg.

More Info

Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EEVSEYCSHM IGSGHLQSLQ RLIDSQMETS CQITFEFVDQ EQLKDPVCYL KKAFLLVQDI MEDTMRFRDN TPNAIAIVQL QELSLRLKSC FTKDYEEHDK ACVRTFYETP LQLLEKVKNV FNETKNLLDK DWNIFSKNCN NSFAECSSQ.

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, His Tag

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

Product # :

CYT-438

Price :

Quantity :

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Shipped with Ice Packs

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Description

CTGF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (27-349) and having a molecular mass of 37.7kDa.The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CTGF protein (1mg/ml) is supplied in 20mM Tris-HCl, pH-8 and 10% Glycerol.

Purity

Greater than 85.0% as determined by Analysis by SDS-PAGE.

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 modulesModule 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, Connective Tissue Growth Factor.
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 MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 37.7kDa.

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

What is the Purity of CTGF Protein?
CTGF Protein is >85% 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?
MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.

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:

Macrophage-Colony Stimulating Factor Rat Recombinant

Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.

Product # :

CYT-856

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Macrophage Colony Stimulating Factor Rat Recombinant produced in E.coli is a non-glycosylated homodimer, containing 2 x 155 amino acids and having a total molecular mass of 36.2 kDa.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile filtered aqueous solution containing 10mM Na3PO4, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity as determined by dose-dependent induction of M-NFS-60 cell proliferation is 1.65 ng/ml. This corresponds to an expected specific activity of 6.1x10⁵ units/mg.

More Info

Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEVSEHCSHM IGNGHLQILQ QLIDSQMETA CLIEYKFVDQ EQLDDPVCYL KKAFVLVQVI IEETMRFKDN TPNANATERL QELSMKLNSC FIKDYKEQNE ACVQTYKESP LRLLEKIKNF FNETKNFLEK DWNIFSKNCN DSLAKCSSRD VVTKP.

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 17 Human Recombinant, His Tag

Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

Product # :

CYT-755

Price :

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Description

FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (23-216 a.a) and having a molecular mass of 25.2kDa.FGF17 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

FGF17 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.
Synonyms
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
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 MGSHMTQGEN HPSPNFNQYV RDQGAMTDQL SRRQIREYQL YSRTSGKHVQ VTGRRISATA EDGNKFAKLI VETDTFGSRV RIKGAESEKY ICMNKRGKLI GKPSGKSKDC VFTEIVLENN YTAFQNARHE GWFMAFTRQG RPRQASRSRQ NQREAHFIKR LYQGQLPFPN HAEKQKQFEF VGSAPTRRTK RTRRPQPLT.
Background
What is the molecular weight/Mw of FGF17 HIS Protein?
FGF17 HIS Protein has a total Mw of 25.2kDa.

What is the source or expression system of FGF17 HIS Protein?
Escherichia Coli.

What is the Purity of FGF17 HIS Protein?
FGF17 HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF17 HIS Protein?
The biological functionality of FGF17 HIS Protein will be determined in the future.

What is the amino acid sequence of FGF17 HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMTQGEN HPSPNFNQYV RDQGAMTDQL SRRQIREYQL YSRTSGKHVQ VTGRRISATA EDGNKFAKLI VETDTFGSRV RIKGAESEKY ICMNKRGKLI GKPSGKSKDC VFTEIVLENN YTAFQNARHE GWFMAFTRQG RPRQASRSRQ NQREAHFIKR LYQGQLPFPN HAEKQKQFEF VGSAPTRRTK RTRRPQPLT.

What applications can FGF17 HIS Protein be used in?
FGF17 HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF17 HIS Protein?
The endotoxin level is minimal, FGF17 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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