Recombinant :
Recombinant FGF-8a, Human Source :
Escherichia coli. Molecular Weight :
21.3 kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE analysis. Biological Activity :
ED50 < 500 ng/mL, measured by a cell proliferation assay using 3T3 cells in the presence of 1 μg/ml of heparin, corresponding to a specific activity of > 2× 10ˆ3 units/mg. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGD PFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR Endotoxin :
< 0.2 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O at 100 μg/mL. Storage :
Lyophilized recombinant human Fibroblast Growth Factor 8a (rhFGF-8a) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-8a remains stable up to 2 weeks at 4°C or up to 3 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Fibroblast Growth Factor 8a (FGF-8a) is a cytokine belonging to the heparin-binding FGF family, which has at least 23 members. FGF-8 has 8 different isoforms, named FGF-8a through FGF-8h. Different FGF-8 isoforms have different affinities to the receptors, and thus participate in different signaling cascade pathways. FGF-8 has very widespread expression during embryonic development, and is an organizer and inducer for gastrulation, somitogenesis, morphogenesis, and limb induction. However, FGF-8 is also a potential oncogene: in normal adult cells, FGF-8 has very low expression, but FGF-8 is highly expressed in cancer cells of breast, prostate, and ovarian tumors. FGF-8 promotes tumor angiogenesis by increasing neovascularization, and induces osteoblastic differentiation. Recombinant human Fibroblast Growth Factor 8a (rhFGF-8a) produced inE.coli is a single non-glycosylated polypeptide chain containing 183 amino acids. A fully biologically active molecule, rhFGF-8a has a molecular mass of 21.3 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.
Recombinant FGF-8a, Human Source :
Escherichia coli. Molecular Weight :
21.3 kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE analysis. Biological Activity :
ED50 < 500 ng/mL, measured by a cell proliferation assay using 3T3 cells in the presence of 1 μg/ml of heparin, corresponding to a specific activity of > 2× 10ˆ3 units/mg. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGD PFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR Endotoxin :
< 0.2 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O at 100 μg/mL. Storage :
Lyophilized recombinant human Fibroblast Growth Factor 8a (rhFGF-8a) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-8a remains stable up to 2 weeks at 4°C or up to 3 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Fibroblast Growth Factor 8a (FGF-8a) is a cytokine belonging to the heparin-binding FGF family, which has at least 23 members. FGF-8 has 8 different isoforms, named FGF-8a through FGF-8h. Different FGF-8 isoforms have different affinities to the receptors, and thus participate in different signaling cascade pathways. FGF-8 has very widespread expression during embryonic development, and is an organizer and inducer for gastrulation, somitogenesis, morphogenesis, and limb induction. However, FGF-8 is also a potential oncogene: in normal adult cells, FGF-8 has very low expression, but FGF-8 is highly expressed in cancer cells of breast, prostate, and ovarian tumors. FGF-8 promotes tumor angiogenesis by increasing neovascularization, and induces osteoblastic differentiation. Recombinant human Fibroblast Growth Factor 8a (rhFGF-8a) produced inE.coli is a single non-glycosylated polypeptide chain containing 183 amino acids. A fully biologically active molecule, rhFGF-8a has a molecular mass of 21.3 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.
Blocking peptide available as BK0045-10μgP