lldD, also known as L-lactate dehydrogenase, is present in a wide variety of organisms, including plants and animals. It is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. As it can also catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).
Source:
Recombinant corresponding to aa1-396 from E.coli lldD, fused to His-tag at N-terminus, expressed in E.coli.
Molecular Weight:
~45.3kD (420aa) confirmed by MALDI-TOF
AA Sequence:
MGSSHHHHHH SSGLVPRGSH MGSHMIISAA SDYRAAAQRI LPPFLFHYMD GGAYSEYTLR RNVEDLSEVA LRQRILKNMS DLSLETTLFN EKLSMPVALA PVGLCGMYAR RGEVQAAKAA DAHGIPFTLS TVSVCPIEEV APAIKRPMWF QLYVLRDRGF MRNALERAKA AGCSTLVFTV DMPTPGARYR DAHSGMSGPN AAMRRYLQAV THPQWAWDVG LNGRPHDLGN ISAYLGKPTG LEDYIGWLGN NFDPSISWKD LEWIRDFWDG PMVIKGILDP EDARDAVRFG ADGIVVSNHG GRQLDGVLSS ARALPAIADA VKGDIAILAD SGIRNGLDVV RMIALGADTV LLGRAFLYAL ATAGQAGVAN LLNLIEKEMK VAMTLTGAKS ISEITQDSLV QGLGKELPAA LAPMAKGNAA
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. 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.
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