Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
recombinant human FGF2.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Fibroblast Growth Factor 2,Bfgf,Fgf-2,Fgfb,Hbgf-2,Fgf2
Fibroblast growth factors (FGFs) are members of a family of polypeptides that are potent regulators of cell proliferation, differentiation and function. The FGF family consists of seven members with 30-50% sequence identity at the amino acid level and with conservation of the positions of two cysteine residues. The factors are designated FGF-1 through FGF-7; the names FGF acidic and basic are used for FGF-1 and FGF-2, respectively. Acidic and basic fibroblast growth factor (aFGF and bFGF, respectively) are members of a small family of heparin binding growth factors (HBGF). Comparisons of the primary structure have shown that aFGF and bFGF are closely related mitogens with 55% homology. When isolated from natural sources, bFGF usually has an apparent mass of about 18 kDa, but a variety of larger forms, up to 24 kDa, can exist. Natural bFGF exists in three forms, the 154 amino-acid form and two truncated versions of 146 and 131 amino acids lacking the N-terminal 9 and 24 residues, respectively. Depending on the organ from which it is purified, either the complete or truncated forms of bFGF may be present. In pituitary and brain the complete form predominates, in kidney and corpus luteum only the truncated form can be detected, and in adrenal glands, both forms coexist. Human and bovine bFGF are nearly identical in sequence, differing at only two positions. The largest (154 aa) form of both human and bovine aFGF share all but 12 amino acids. FGFs play crucial roles in normal development, in the maintenance of tissues, and in wound healing and repair. They have been implicated in a wide range of pathological conditions, including tumorigenesis and metastasis. Both aFGF and bFGF exert their mitogenic influence via saturable high-affinity receptors on a variety of cells of mesodermal and neuroectodermal origin, including endothelial cells, smooth muscle cells, fibroblasts, gliomas, chondrocytes, hepatocytes, epithelial cells, and myoblasts. As expected from the sequence homology between the acidic and basic forms of FGF and from their ability to support the proliferation in vitro of the same spectrum of target cells, both aFGF and bFGF interact with the same cell surface receptor.