Recombinant :
Recombinant VEGF164, Rat (P. pastoris-expressed) Source :
P. pastoris Molecular Weight :
38 kDa, observed by non-reducing SDS-PAGE. Purity :
> 95% as analyzed by reducing SDS-PAGE. Biological Activity :
ED50<4 ng/ml, measured by cell proliferation assay of HUVEC. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MAPTTE GEQKAHEVVK FMDVYQRSYC RPIETLVDIF QEYPDEIEYI FKPSCVPLMR CAGCCNDEAL ECVPTSESNV TMQIMRIKPH QSQHIGEMSF LQHSRCECRP KKDRTKPENH CEPCSERRKH LFVQDPQTCK CSCKNTDSRC KARQLELNER TCRCDKPRR Endotoxin :
<1 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O or PBS at 100 μg/ml. Storage :
Lyophilized recombinant rat Vascular Endothelial Growth Factor A164(rrVEGF-A164) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rrVEGF-A164 should be stable up to 1 week at 4°C or up to 2 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 :
Vascular Endothelial Growth Factor A164 (VEGF-A164), a member of the cysteine knot growth factor[1], is one of major isoforms of VEGF-As. VEGF-As are endothelial cell-specific mitogens with angiogenic and vascular permeability-inducing properties[2]. During maturation, rat VEGF-A is alternatively spliced to generate rVEGF-A120, rVEGF-A164 and rVEGF-A188[3] which correspond to hVEGF-A121, hVEGF-A165 and hVEGF-A189 in human, respectively (the numbers designate the amino acid residues). The active form of rVEGF-A164 is either a homodimeric or heterodimeric polypeptides which bind to the transmembrane tyrosine kinases receptors FLT1, FLK1 or KDR[4] or to the non-tyrosine kinase neuropilin receptors NRP1/2[5].Recombinant rat Vascular Endothelial Growth Factor A164 (rrVEGF-A164) produced in P. pastoris is a disulfide-linked homodimer containing two polypeptide chains of 165 amino acids each. A fully biologically active molecule, rrVEGF-A164 has a molecular mass of 38 kDa analyzed by non-reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.
Recombinant VEGF164, Rat (P. pastoris-expressed) Source :
P. pastoris Molecular Weight :
38 kDa, observed by non-reducing SDS-PAGE. Purity :
> 95% as analyzed by reducing SDS-PAGE. Biological Activity :
ED50<4 ng/ml, measured by cell proliferation assay of HUVEC. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MAPTTE GEQKAHEVVK FMDVYQRSYC RPIETLVDIF QEYPDEIEYI FKPSCVPLMR CAGCCNDEAL ECVPTSESNV TMQIMRIKPH QSQHIGEMSF LQHSRCECRP KKDRTKPENH CEPCSERRKH LFVQDPQTCK CSCKNTDSRC KARQLELNER TCRCDKPRR Endotoxin :
<1 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O or PBS at 100 μg/ml. Storage :
Lyophilized recombinant rat Vascular Endothelial Growth Factor A164(rrVEGF-A164) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rrVEGF-A164 should be stable up to 1 week at 4°C or up to 2 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 :
Vascular Endothelial Growth Factor A164 (VEGF-A164), a member of the cysteine knot growth factor[1], is one of major isoforms of VEGF-As. VEGF-As are endothelial cell-specific mitogens with angiogenic and vascular permeability-inducing properties[2]. During maturation, rat VEGF-A is alternatively spliced to generate rVEGF-A120, rVEGF-A164 and rVEGF-A188[3] which correspond to hVEGF-A121, hVEGF-A165 and hVEGF-A189 in human, respectively (the numbers designate the amino acid residues). The active form of rVEGF-A164 is either a homodimeric or heterodimeric polypeptides which bind to the transmembrane tyrosine kinases receptors FLT1, FLK1 or KDR[4] or to the non-tyrosine kinase neuropilin receptors NRP1/2[5].Recombinant rat Vascular Endothelial Growth Factor A164 (rrVEGF-A164) produced in P. pastoris is a disulfide-linked homodimer containing two polypeptide chains of 165 amino acids each. A fully biologically active molecule, rrVEGF-A164 has a molecular mass of 38 kDa analyzed by non-reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.
Blocking peptide available as BK0351-10μgP