Recombinant FGF-8, Human 
Datasheet
COA
MSDS
SHIP
Recombinant :
Recombinant FGF-8, Human Source :
Escherichia coli. Molecular Weight :
22.5kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE and HPLC analyses. Biological Activity :
ED50 < 5.0 ng/ml, measured by a cell proliferation assay using 3T3 cells in the presence of 1μg/ml of heparin, corresponding to a specific activity of > 2.0× 10ˆ5 units/mg. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MQVTVQSSPN FTQHVREQSL 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-8 (rhFGF-8) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-8 should be 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-8 (FGF-8) is a heparin-binding growth factor of the FGF family. There are 4 known forms of FGF8 produced by alternative splicing: FGF8a, FGF-8b, FGF-8e and FGF-8f. The human and mouse FGF8b are identical of aa sequences. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF-8 is required for normal brain, eye, ear and limb development during embryogenesis. It is also required for normal development of the gonadotropin- releasing hormone (GnRH) neuronal system.Recombinant human Fibroblast Growth Factor-8 (rhFGF-8) produced in E.coli is a single non-glycosylated polypeptide chain containing 194 amino acids. A fully biologically active molecule, rhFGF-8 has a molecular mass of 22.5kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.
Recombinant FGF-8, Human Source :
Escherichia coli. Molecular Weight :
22.5kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE and HPLC analyses. Biological Activity :
ED50 < 5.0 ng/ml, measured by a cell proliferation assay using 3T3 cells in the presence of 1μg/ml of heparin, corresponding to a specific activity of > 2.0× 10ˆ5 units/mg. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MQVTVQSSPN FTQHVREQSL 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-8 (rhFGF-8) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-8 should be 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-8 (FGF-8) is a heparin-binding growth factor of the FGF family. There are 4 known forms of FGF8 produced by alternative splicing: FGF8a, FGF-8b, FGF-8e and FGF-8f. The human and mouse FGF8b are identical of aa sequences. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF-8 is required for normal brain, eye, ear and limb development during embryogenesis. It is also required for normal development of the gonadotropin- releasing hormone (GnRH) neuronal system.Recombinant human Fibroblast Growth Factor-8 (rhFGF-8) produced in E.coli is a single non-glycosylated polypeptide chain containing 194 amino acids. A fully biologically active molecule, rhFGF-8 has a molecular mass of 22.5kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.
Blocking peptide available as BK0044-10μgP