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R&D Systems/Recombinant Human FGF basic (146 aa) Protein/233-FB-01M/1 mg

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233-FB-01M-1mg

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Purity>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.Endotoxin LevelActivityMeasured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.1-0.6 ng/mL.The specific activity of Recombinant Human FGF basic is approximately 800 IU/μg, which is calibrated against recombinant human FGF basic WHO International Standard (NIBSC code: 90/712).SourceE. coli-derived Pro143-Ser288, with an N-terminal AlaAccession #P09038 N-terminal Sequence AnalysisAla-Pro143Predicted Molecular Mass16.5 kDaSDS-PAGE17 kDa, reducing conditions References:Coulier, F. et al. (1997) J. Mol. Evol. 44:43.Chen, C.H. et al. (2004) Curr. Vasc. Pharmacol. 2:33.Mohammadi, M. et al. (2005) Curr. Opin. Struct. Biol. 15:506.Fernig, D. et al. (1994) Prog. Growth Factor Res. 5:353.Long Name:Fibroblast Growth Factor basicEntrez Gene IDs:2247 (Human); 14173 (Mouse); 281161 (Bovine); 403857 (Canine); 100033955 (Equine)Alternate Names:basic fibroblast growth factor bFGF; Basic fibroblast growth factor; bFGF; FGF basic; FGF2; FGF-2; FGF2AS; FGFBprostatropin; fibroblast growth factor 2 (basic); GFG1; HBGF-2; HBGH-2; heparin-binding growth factor 2; NUDT6; ProstatropinBackground:FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum, and placenta. This factor contains four cysteine residues, but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. A variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. Binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF basic stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates embryonic development and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may participate in the production of a variety of pathological conditions resulting from excessive cell proliferation and excessive angiogenesis.

R&D Systems位于美国的明尼苏达州，一直致力于生物制品的开发与生产。公司成立之初主要生产用于医院及临床应用的血控品。1997年，公司推出第一个产品--富血小板血浆质控品；1981年，公司成为全球第二家生产含血小板全血控品的供应商。40多年的发展中，R&D Systems仍持续开发各种血控品产品。

1985年，作为公司推出的第一个科研试剂产品，也是全球第一家将该产品进行商业化生产的产品，R&D Systems成功上市了TGF-beta1蛋白。作为胞外信号分子，TGF-beta1蛋白在多种细胞中进行表达，并作为胞外信号分子参与免疫功能，细胞增殖和细胞分化等生物学过程。该产品推出后，公司陆续从生物材料中纯化了几种细胞因子产品并推向市场。

天然蛋白类产品的成功推广，加速了R&D Systems在细胞因子市场的开拓。公司于1985年形成Growth Factor事业部（现Biotechnology事业部）。Biotechnology事业部的目标是生产和营销重组人细胞因子。与天然来源提取蛋白相比较，DNA重组技术生产的蛋白产品其成本更低，产量更高，完全摆脱原料的限制。1989年，Biotechnology事业部开始开发抗细胞因子的单克隆和多克隆抗体，并于1990年开发了第一个ELISA试剂盒。

2014年2月10日，R&D Systems的母公司宣布命名为Bio-Techne. Bio-Techne旗下包括R&D Systems, Novus Biologicals, BiosPacific, Tocris Bioscience, Boston Biochem和Bionostics。