fgf2

Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. FGF-2 Protein, Chicken, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 18.3 kDa and the accession number is P48800.

FGF-2 Protein, Human, Recombinant (K128N) is expressed in E. coli expression system. The predicted molecular weight is 17 KDa and the accession number is P09038-2.

FGF-2 Protein, Human,Recombinant (Q65I, C96S, N111G) is expressed in E. coli expression system. The predicted molecular weight is 16 KDa and the accession number is P09038-2.

FGF basic is one of 22 mitogenic proteins of the FGF family, which show 35-60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. The 17 kDa mouse sequence has 98% aa identity with rat, and 95% identity with human, bovine, and sheep FGF basic. Binding of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids with lower affinity. Expression of FGF basic is nearly ubiquitous but disruption of the mouse FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF family members. FGF basic modulates such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, neuronal function and neural degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and angiogenesis is reminiscent of a variety of pathological conditions.

FGF-basic is a members of the Fibroblast Growth Factors (FGFs) family. The family constitutes a large family of proteins involved in many aspects of development including cell proliferation, growth, and differentiation. They act on several cell types to regulate diverse physiologic functions including angiogenesis, cell growth, pattern formation, embryonic development, metabolic regulation, cell migration, neurotrophic effects, and tissue repair. FGF-basic is a non-glycosylated heparin binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4.

Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. FGF-2 Protein, Chicken, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 23.8 kDa and the accession number is P48800.

Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Binds to integrin ITGAV:ITGB3. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. Mediates phosphorylation of ERK1 2 and thereby promotes retinal lens fiber differentiation. FGFb Protein, Rabbit, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 28.4 kDa and the accession number is P48799.

FGF-2 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 16.5 kDa and the accession number is P09038-4.

FGF-2 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 18.5 kDa and the accession number is P15655.

Glypican-5 (GPC5), is a cell membrane protein that belongs to the glypican family. The glypicans compose a family of glycosylphosphatidylinositol-anchored heparan sulfate proteoglycans that may play a role in the control of cell division and growth regulation. So far, six members (Glypican-1 GPC1, Glypican-2 GPC2, Glypican-3 GPC3, Glypican-4 GPC4, Glypican-5 GPC5, Glypican-6 GPC6) of this family are known in the vertebrates. In the adult, Glypican-5 is primarily expressed in the brain. It is also detected in the fetal brain, lung, and liver. Glypican-5 enhances the intracellular signaling of FGF2 and HGF. It alters the cellular distribution of FGF2. The properties of Glypican-5 make it an attractive target for therapeutic intervention in rhabdomyosarcomas and other tumors that amplify and or overexpress its gene. Glypican-5 is overexpressed in lymphoma cell lines that had shown amplification. It is a likely target for amplification, and that over-expression of GPC5 may contribute to the development and or progression of lymphomas and other tumors.

Glypican-1 is a cell membrane protein and belongs to the glypican family. The protein may act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. It is required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling.