Recombinant human GAPDH protein

Specific activity is > 50unit/mg, and is defined as the amount of enzyme that convert 1.0 umole of glyceraldehyde-3-phosphate to 1, 3-Bisphosphoglycerate per minute at pH 8.5 at 37C.

MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer composed of 36-kDa subunits and has various intracellular functions. GAPDH catalyzes the reversible reduction of 1, 3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, evidence suggests that mammalian GAPDH is also involved in a great number of intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. Recombinant GAPDH protein was expressed in E. coli and purified by using conventional chromatography techniques.

E.coli

Enzymes & Proteases

36 kDa (335aa) confirmed by MALDI-TOF