LDHA, also known as L-lactate dehydrogenase A chain, is an enzyme that catalyzes the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. This protein is found predominantly in muscle tissue and belongs to the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. Source: Recombinant protein corresponding to aa1-332 from human LDHA, fused to His-tag at N-terminal expressed in E. coli. Molecular Weight: ~38.8kD (352aa) Specific Activity: >300units/mg, in which one unit will convert 1umole of pyruvate to L-lactate and beta-NAD/minute at pH 7.5 at 37C. Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
