Recombinant Human FGF-Acidic

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Pricing & Details

Product. No.F112
Alternate Names
Fibroblast Growth Factor-Acidic, FGF-1, ECGF, HBGF-1, AFGF, ECGF-Beta, ECGFA, ECGFB, FGF-Alpha, FGFA, GLIO703
Expression Host
E. coli
Species
Human
Prod No.
Size
Price
Avail.
Qty
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F112-25 µg
25 µg
$189.00
In stock
Max:
Min: 1
Step: 1

Background

Acidic fibroblast growth factor (aFGF), also known as FGF-1, ECGF and HBGF-1, is a non-glycosylated heparin binding growth factor and member of the FGF family of mitogenic peptides. It is involved in several important physiological and pathological processes, such as embryonic development, morphogenesis, angiogenesis, wound healing and atheromatosis (1). aFGF is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. It is the only member of the FGF family that binds with high affinity to all four FGF receptors (2). aFGF binds to cell surface receptors with high affinity with the prerequisite association with heparan sulfate. This ligation subsequently initiates receptor dimerization, transphosphorylation, as well as internalization of receptor/FGF complexes, and thus aFGF is translocated across cellular membranes and transported to the nucleus. The FGF pathway regulates primitive hematopoiesis by modulating transcription factors such as Gata1 expression level and activity (3). aFGF has been implicated in an autocrine system by which calcium regulates parathyroid cell growth. It has been demonstrated that the expression of aFGF is highest during the late stages of hepatic morphogenesis in newborn rats as well as during hepatic differentiation in adult liver. The intravenous application of aFGF has shown that the factor promotes the regeneration of the endothelium following arterial intravascular injuries (4). Overexpression of aFGF in pancreatic cancers has been found to be associated with a more advanced tumor stage. Recent studies have also demonstrated that chimeric toxins composed of aFGF fused to mutant forms of Pseudomonas exotoxin, are cytotoxic to a variety of tumor cell lines with FGF receptors (5).

Protein Details

Purity
>97% by SDS-PAGE and analyzed by silver stain.
Endotoxin Level
<0.01 EU/µg as determined by the LAL method
Biological Activity
The biological activity of Human FGF-acidic was determined by its ability to stimulate 3H-thymidine incorporation in quiescent NR6R-3T3 fibroblasts (Rizzino, A. et al., 1988, Cancer Research 48:4266 - 4271). The expected ED50 for this effect is typically 0.1 - 0.3 ng/ml in the presence of 10 μg/ml of heparin.
Expression Host
E. coli
Protein Accession No.
NP_000791
Amino Acid Sequence
fnlppgnykk pkllycsngg hflrilpdgt vdgtrdrsdq hiqlqlsaes vgevyikste tgqylamdtd gllygsqtpn eeclflerle enhyntyisk khaeknwfvg lkkngsckrg prthygqkai lflplpvssd
N-terminal Sequence Analysis
Met
State of Matter
Lyophilized
Predicted Molecular Mass
The predicted molecular weight of Recombinant Human FGF-acidic is Mr 15.5 kDa.
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Country of Origin
USA
Shipping
Next Day Ambient
NCBI Gene Bank

References & Citations

1. Jaye, M. et al. (1986) Science 233:541
2. Otlewski, J. et al. (2009) Acta. Crystallogr. D. Biol. Crystallogr. 65:67
3. Nakazawa, F. et al. (2006) Blood. 108:3335
4. Bjornsson, TD. et al. (1991) Proc. Natl. Acad. Sci. (USA) 88:8651
5. Merwin, JR. et al. (1992) Cancer Res. 52:4995
IMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein.
Products are for research use only. Not for use in diagnostic or therapeutic procedures.
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