Download Recombinant Human Fibroblast Growth Factor, acidic (rhFGFa

rhFGFa
Recombinant Human Fibroblast Growth Factor, acidic
(rhFGFa)
(Catalog # P017)
Description:
Acidic Fibroblast Growth Factor (FGF) is also called FGF-1, HBGF-1 (Heparin Binding Growth Factor protein), an
endothelia cell growth factor. FGF family comprises of seven related mitogenic proteins that have 30-50% amino ac
conservation. Acidic and basic FGFs have similar molecular weights, biological activities and approximately 55% a
acid homology. Unlike the other members of the family, they lack signal peptides and are apparently secreted by
mechanisms other than the classical protein secretion pathway. Acidic FGF has been found in brain, retina, bone ma
osteosarcoma cells. FGF contains three cysteine residues, but the reduced form retains full biological activity, indica
disulfide bonds are not required activities. Two general types of surface receptors have been identified that bind acid
basic FGF. These are the low affinity heparin sulfate proteoglycans (HsPGs) and high affinity receptors that are
transmembrane proteins with tyrosine kinase activity. The biological activity of rhFGFa is greatly enhanced in vitro
addition of heparin. Recent studies indicate that binding at FGFa to heparin or cell surface heparin sulfate proteogly
necessary for binding of FGFa to high affinity FGF receptors.
The nucleotide sequence of human FGFa cDNA predicts a 155 amino acid residue protein. However, as a result of
purification artifacts, the human FGFa initially purified and characterized from natural sources was shown to be a 14
amino acid residue protein due to amino terminal truncations of the first 15 amino acid residues. A DNA sequence e
the 140 amino acid residue amino-terminally truncated form of human FGF acidic was express in E. coli expression
prepared from freshly extracted cell lysates, and purified to homogeneity via sequential chromatography. The predic
molecular weight of rhFGFa is 15.8 KDa. The The final fraction of enzyme contains single polypeptide band of
approximately 16 kDa on SDS PAGE.
Purity:
>95% as determined by SDS-PAGE and HPLC analysis.
Endotoxin:
<0.1 ng/µg.
Reconstitution recommendations:
Reconstitute in ddWater supplemented with 0.1% BSA to a concentration of 1.0 mg/ml. This is protein is not stable
buffer concentration or low pH. Stock solutions should be apportioned into working aliquots and stored at <-20ºC. I
dilute solution required, it is suggested that they be made in a buffered solution containing carrier protein such as PB
0.1% BSA.
Storage:
The final fraction of rhFGFa is protein carrier free and lyophilized from a solution containing 1mg/ml rhFGFa, 10m
(pH7.6), and 0.1M NaCl. Lyophilized rhFGFa is stable at 4ºC. In general, rhFGFa is less stable when diluted with lo
and low buffer. Please follow the given reconstitution recommendations. We don’t recommend any further dilution
rhFGFa beyond 1mg/ml for an extensive storage. After reconstitution, please store rhFGFa at -20ºC or lower. In add
rhFGFa
is a good practice to aliquot rhFGFa after the first thaw and keep freeze-thaw cycles to a minimum.
Biological Activity:
ED50 <10ng/ml (>1x105 units/mg). Biological activity is determined by measuring the FGFa dose dependent stimul
3H-thymidine
incorporation in quiescent NR6R-3T3 cell fibroblasts. For most in vitro applications, a concentration
1.0-50 ng/ml is recommended. FGFa is a heparing-binding protein which stimulates the proliferation of mesenchym
neuroectodermal cells, and endothelia cells.
Shipping:
The lyophilized rhFGFa shall be shipped on ice and the reconstituted rhFGFa must be shipped at -20ºC or lower.
Legal consideration: FOR RESEARCH USE ONLY, NOT FOR THERAPEUTIC PURPOSE.
Reference:
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Neurobiol. 1994 Feb;4(1):78-86. Review. PMID: 8173328.
Cuevas P, Reimers D, Carceller F, Martinez-Coso V, Redondo-Horcajo M, Saenz de Tejada I, Gimenez-Gallego G.
Fibroblast growth factor-1 prevents myocardial apoptosis triggered by ischemia reperfusion injury. Eur J Med Res.
Nov 28;2(11):465-8. PMID: 9385115.
Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA. The complete amino acid sequence of human brain-derived
fibroblast growth factor. Biochem Biophys Res Commun. 1986 Jul 31;138(2):611-7.
Gospodarowicz D, Cheng J, Lui GM, Baird A, Bohlent P. Isolation of brain fibroblast growth factor by heparin-Sep
affinity chromatography: identity with pituitary fibroblast growth factor. Proc Natl Acad Sci U S A. 1984 Nov;81(2
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Harper JW, Strydom DJ, Lobb RR. Human class 1 heparin-binding growth factor: structure and homology to bovine
brain fibroblast growth factor. Biochemistry. 1986 Jul 15;25(14):4097-103. PMID: 2427112.
Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN. Hum
endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization. Science. 1986 Aug 1;23
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Junttila T, Rechardt L, Cao Y, Hokfelt T, Pelto-Huikko M. Distribution of acidic fibroblast growth factor-like
immunoreactivity in rat skeletal muscle fibers. Brain Res. 1996 Jan 22;707(1):81-7. PMID: 8866716.
Matuo Y, Nishi N, Muguruma Y, Yoshitake Y, Masuda Y, Nishikawa K, Wada F. Stabilization of fibroblast growth
by a non-cytotoxic zwitterionic detergent, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate (CHAPS
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Rizzino A, Kazakoff P, Ruff E, Kuszynski C, Nebelsick J. Regulatory effects of cell density on the binding of transf
growth factor beta, epidermal growth factor, platelet-derived growth factor, and fibroblast growth factor. Cancer Re
Aug 1;48(15):4266-71. PMID: 3260536.