Angiogenesis plays a fundamental role in the growth of solid tumors. A family of angiogenic factors has been described which includes the basic and acidic fibroblast growth factors (bFGF and aFGF). As with other angiogenic factors bFGF will bind to heparin, has mitogenic properties and is a chemo-attractant for cells derived from the mesenchyme. A factor similar to bFGF has been described in the urine of patients with kidney or bladder cancer. A cDNA and a genomic clone for bFGF has been described. Data from the cDNA clones indicate that the bFGF protein is 155 amino acids in length with a putative molecular weight of 17.8kD. bFGF purified from human placenta has an additional 2 amino acids N-terminal to the initiating methionine. A 25kD species of bFGF has been described in guinea pig brain extracts and Florkiewicz and Sommer have described multiple molecular weight forms of bFGF in the human hepatoma cell line SK-HEP-1. bFGF is modified by phosphorylation on Thr-112 by protein kinase A and on Ser-64 by protein kinase C. Phosphorylation of Thr-112 appears to be important in ligand-receptor interaction.
Applications:
Suitable for use in ELISA. Other applications not tested.
Recommended Dilution:
Optimal dilutions to be determined by the researcher.
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Reconstitute with sterile 40-50% glycerol, aliquot and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.