Human Fibroblast Growth Factor 2 (FGF-2)-GST Protein
This recombinant human FGF-2 is expressed as a GST-fusion protein, which allows for easy detection via western blot. The fusion junction of the protein harbors an engineered thrombin cleavage site and a protein kinase A (PKA) phosphorylation site. The GST portion of the fusion protein can be cleaved off by thrombin if necessary. The fusion protein can be radioactively labeled with 32P-r-ATP and PKA.
Fibroblast growth factor-2 (FGF-2 or b-FGF) belongs to the FGF family of more than 20 growth factors possessing broad mitogenic and angiogenic activities through differential interactions with four major tyrosine kinase FGF receptors. Cross-talk mechanisms exist among FGF-2 and different members of the VEGF family during angiogenesis and vasculogenesis. This property has implicated FGF-2 in diverse areas of preclinical studies such as tumor growth, vascular and bone remodeling, and cardiac hypertrophy. Multiple forms of FGF-2 are generated by alternative translation on the same mRNA transcript, producing a low molecular weight (LMW ~18 kDa) and several high molecular weight (HMW 20-24 kDa) forms from AUG (methionine) and CUG (leucine) codons, respectively. All FGF-2 forms lack a classical signal peptide that directs secretion through the endoplasmic reticulum-Golgi pathway.
From the laboratory of Te-Chung Lee, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
This recombinant human FGF-2 is expressed as a GST-fusion protein, which allows for easy detection via western blot. The fusion junction of the protein harbors an engineered thrombin cleavage site and a protein kinase A (PKA) phosphorylation site. The GST portion of the fusion protein can be cleaved off by thrombin if necessary. The fusion protein can be radioactively labeled with 32P-r-ATP and PKA.
Fibroblast growth factor-2 (FGF-2 or b-FGF) belongs to the FGF family of more than 20 growth factors possessing broad mitogenic and angiogenic activities through differential interactions with four major tyrosine kinase FGF receptors. Cross-talk mechanisms exist among FGF-2 and different members of the VEGF family during angiogenesis and vasculogenesis. This property has implicated FGF-2 in diverse areas of preclinical studies such as tumor growth, vascular and bone remodeling, and cardiac hypertrophy. Multiple forms of FGF-2 are generated by alternative translation on the same mRNA transcript, producing a low molecular weight (LMW ~18 kDa) and several high molecular weight (HMW 20-24 kDa) forms from AUG (methionine) and CUG (leucine) codons, respectively. All FGF-2 forms lack a classical signal peptide that directs secretion through the endoplasmic reticulum-Golgi pathway.
From the laboratory of Te-Chung Lee, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Protein |
| Name: | Human Fibroblast Growth Factor 2 (FGF-2)-GST |
| Accession ID: | NM_002006 |
| Source: | Recombinant, purified from E. coliBL21 |
| Molecular Weight: | 17.3 kDa (~40kDa with GST) |
| Amino Acid Sequence: | MAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS |
| Fusion Tag(s): | GST |
| Purity: | 99% |
| Buffer: | PBS |
| Concentration: | 0.1mg/mL |
| Storage: | Store at -80C |
| Shipped: | Dry ice |
FGF-2 Activity Analysis
FGF-2 activity assessed by its ability to stimulate cell proliferation. The figure shows FGF-2-mediated stimulation of C2C12 myocyte proliferation. Cells were treated with the indicated concentrations of GST-FGF-2 for 3 days in the absence of serum, and MTT assay was performed to measure cell growth. The figure shows that maximal growth stimulation was achieved at a GST-FGF-2 concentration of ~10 ng/ml.
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