FGF2 (BFGF, Heparin-binding Growth Factor 2, HBGF-2, Basic Fibroblast Growth Factor, bFGF, FGFB)

FGF basic (FGF2) is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. FGF2 is involved in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. FGF2 mRNA 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.\n\nApplications:\nSuitable for use in Neutralization Assay. Other applications not tested.\n\nRecommended Dilution:\nNeutralization: 2.5ug/ml\nOptimal dilutions to be determined by the researcher.\n\nPositive Control:\nFBHE cells\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

029476

Size

100ug

Hosts

Mouse

Reactivities

Bov

Form

Supplied as a liquid in PBS. No preservative added.

P Type

Mab

Purity

Purified by Protein G affinity chromatography.

Isotype

IgG1,k

References

1. Santiago, J.J., et al. (2010). Cardiovasc Res. 89(1):139-147. 2. Candela, M.E., et al. (2010). J. Cell Physiol. 224(1):144-151. 3. Kobayashi, T., et al. (2007). J. Biol Chem. 282(27):19589-19597. 4. Vincent, T.L., et al. (2007). Osteoarthritis Cartilage. 15(7):752-763. 5. Yanagihara, K., et al. (2004). Cancer Sci. 95(7):575-582. 6. Liu, J., et al. (2003). Am J Physiol Lung Cell Mol Physiol. 285(5):L1106-1115. 7. Dowd, C.J., et al. (1999). J. Biol Chem. 274(8): 5236-5244. 8. Flores, C., et al. (1998). J. Neurosci. 18(22): 9547-9555. 9. Gu, X., et al. (1998). Invest Opthalmol Vis Sci. 39(12):2252-2258. 10. Bugra, K., and Hicks, D. (1997). J. Mol Neurosci. 9(1):13-25. 11. Faries, P.L., et al. (1996). J Vasc Surg. 24(3): 463-741. 12. Fleming, M.G., et al. (1992). Am J Dermatopathol. 22(6):496-502. 13. Fu, Y.M., et al. (1991). J. Cell Biol. 114(6): 1261-1273. 14. Matsuzaki, K., et al. (1989). Proc Natl Acad Sci USA. 86(24):9911-9915. 15. Uteza, Y., et al. (1999). Proc Natl Acad Sci USA. 96(6):3126-3131. 16. Fox, J.C., and Shanley, J.R. (1996). J Bio Chem. 271(21):12578-12584. 17. Gupta, A., et al. (1997). Biol Reprod. 56(6): 1527-1536. 18. Samanthanam, C.A., et al. (1998). Biol Reprod. 59(3):491-496.

Additional Info

Recognizes bovine FGF2. Species sequence homology: human