DescriptionRecombinant HBsAg adw antigen was mutated by replacing the Glutamine residue at position 129 with Histidine.SourcePichia pastoris.Physical AppearanceSterile Filtered clear solution.FormulationSterile Filtered solution containing 20mM
DescriptionRecombinant HBsAg adw antigen was mutated by replacing the Proline residue at position 142 with Serine.SourcePichia pastoris.Physical AppearanceSterile Filtered clear solution.FormulationSterile Filtered solution containing 20mM Na2HPO4,
DescriptionRecombinant HBsAg adw antigen was mutated by replacing the Methionine residue at position 133 with Leucine.SourcePichia pastoris.Physical AppearanceSterile Filtered clear solution.FormulationSterile Filtered solution containing 20mM
DescriptionRecombinant HBsAg adw antigen was mutated by replacing the Methionine residue at position 133 with Histidine.SourcePichia pastoris.Physical AppearanceSterile Filtered clear solution.FormulationSterile Filtered solution containing 20mM
DescriptionRecombinant HBsAg adw antigen was mutated by replacing the Lysine residue at position 141 with Glutamate.SourcePichia pastoris.Physical Appearance.Sterile Filtered clear solutionFormulationSterile Filtered solution containing 20mM Na2HPO4,
DescriptionHbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.SourcePichia Pastoris.Physical AppearanceSterile Filtered pale solution.FormulationSterile Filtered solution containing 20mM
DescriptionRecombinant HBsAg adr produced in CHO cells, the molecular weight is approximately 23-27kDa.SourceCHO.Physical AppearanceSterile Filtered clear solution.FormulationSterile Filtered solution containing 20mM PB and 154mM NaCl.StabilityHBsAg
DescriptionRecombinant HBsAg adr full length monomeric protein contains 227 amino acids of the S-gene a molecular weight of 24 kDa. Small amounts of dimer and trimer forms also exist in the solution.SourceSaccharomyces cerevisae.Physical
DescriptionRecombinant e antigen consists of HBV e immunodominant region containing 10 precore residues at its N-terminus and 1-149 residues from the end of precore to its C-terminus. HBV e-Antigen was expressed from E.coli, the purified recombinant
DescriptionThe E.coli derived 14kDa recombinant protein contains the HBV core delta ayw immunodominant region amino acids 1-144.Purification MethodPurified by proprietary chromatographic technique.PurityHBV Core Delta protein is >95% pure as
DescriptionThe E.Coli derived 18 kDa recombinant protein contains the HBV core ayw immunodominant region, amino acids 1-183.Purification MethodHBV Core protein was purified by proprietary chromatographic technique.PurityHBV Core protein is >95% pure
DescriptionThe E.Coli derived 51.2 kDa recombinant protein contains the VP1-P2A immunodominant regions, amino acids 722-830.Purification MethodInclusion bodies.PurityHAV VP1-P2A protein is >90% pure as determined by 10% PAGE (coomassie