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Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

Support: 877-678-TECH (8324)

Web: [email protected] cellsignal.com

3 Trask LaneDanversMassachusetts01923USA
For Research Use Only. Not for Use in Diagnostic Procedures.
MW (kDa):

16

UniProt ID:

#P05230

Entrez-Gene Id:

2246

Background

FGF acidic is a potent growth factor for fibroblasts and endothelial cells (1). FGF acidic is involved in wound repair, angiogenesis, and development (1). FGF acidic is secreted from cells via an endoplasmic reticulum/Golgi independent mechanism (1,2). The ability of FGF acidic to bind to heparin sulfate is required for its ability to interact with FGF receptors and induce signaling (1-4). There are four distinct FGF receptors and each has multiple splice variants (1,3). FGF acidic binds with high affinity to many, but not all, FGFRs (1). Signaling cascades activated through FGF basic binding to FGFR include the ras-raf-MAPK, PLCγ/PKC, and PI3K/Akt pathways (1).

  1. Powers, C.J. et al. (2000) Endocr Relat Cancer 7, 165-97.
  2. Prudovsky, I. et al. (2003) J Cell Sci 116, 4871-81.
  3. Ornitz, D.M. and Itoh, N. (2001) Genome Biol 2, REVIEWS3005.
  4. Mohammadi, M. et al. (2005) Curr Opin Struct Biol 15, 506-16.

Endotoxin

Less than 0.01 ng endotoxin/1 μg hFGF acidic.

Purity

>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hFGF acidic. All lots are greater than 98% pure.

Source / Purification

Recombinant human FGF acidic (hFGF acidic) Phe16-Asp155 (Accession #NP_000791) was produced in E.coli at Cell Signaling Technology.

Bioactivity

The bioactivity of recombinant hFGF acidic was determined in a NIH/3T3 cell proliferation assay. The ED50 of each lot is between 7-20 pg/ml.

Background

FGF acidic is a potent growth factor for fibroblasts and endothelial cells (1). FGF acidic is involved in wound repair, angiogenesis, and development (1). FGF acidic is secreted from cells via an endoplasmic reticulum/Golgi independent mechanism (1,2). The ability of FGF acidic to bind to heparin sulfate is required for its ability to interact with FGF receptors and induce signaling (1-4). There are four distinct FGF receptors and each has multiple splice variants (1,3). FGF acidic binds with high affinity to many, but not all, FGFRs (1). Signaling cascades activated through FGF basic binding to FGFR include the ras-raf-MAPK, PLCγ/PKC, and PI3K/Akt pathways (1).

Background References

    Cross-Reactivity Key

    H: human M: mouse R: rat Hm: hamster Mk: monkey Vir: virus Mi: mink C: chicken Dm: D. melanogaster X: Xenopus Z: zebrafish B: bovine Dg: dog Pg: pig Sc: S. cerevisiae Ce: C. elegans Hr: horse GP: Guinea Pig Rab: rabbit All: all species expected

    Trademarks and Patents

    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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    Revision 1
    #5234

    Human FGF acidic (hFGF acidic)

    Human FGF acidic (hFGF acidic): Image 1 Expand Image
    The proliferation of NIH/3T3 cells treated with increasing concentrations of hFGF acidic was assessed in the presence of 10 µg/ml heparin. After 24 hr treatment, cells were labeled with BrdU for 4 hrs. BrdU incorporation was determined by ELISA and the OD450-OD690 was determined.
    Human FGF acidic (hFGF acidic): Image 2 Expand Image
    The purity of recombinant hFGF acidic was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant hFGF acidic and staining overnight with Coomassie Blue.
    Human FGF acidic (hFGF acidic): Image 3 Expand Image
    Western blot analysis of extracts from NIH/3T3 cells, untreated or treated with human FGF acidic for 10 minutes, using Phospho-CREB (Ser133) Antibody #9191 (upper) or CREB Antibody #9192 (lower).