Branched chain aminotransferase (BCAT2; EC 220.127.116.11) is an aminotransferase enzyme which acts upon branched-chain amino acids. It uses largely α-ketoglutarate in forming branched chain α-keto acids and glutamate. The biological function of branched chain aminotransferases is to catalyse the synthesis of the branched chain amino acids leucine, isoleucine, and valine.
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|Molecular Weight:||44.03 kDa|
|Buffer:||50 mM potassium phosphate pH-7.4, 50 mM sodium chloride, 0.5 mM ethylenediaminetetraaceticacid, and 2.5% glycerol.|
|Comments:||Human branch-chained aminotransferase-2 , (Accession No. BC004243), aa 390 (full length minus the first 16 aa) with N-terminal hexahistidine tag, MW= 44.01 kDa, expressed in E.coli.|
|Storage:||Stable > 6 months at -80C|
Specific Activity: 10.7 pmol/min/ug. One unit is defined as the amount of enzyme that will convert 1 nmol of NADP to NADPH at 30C. Assay conditions: 100 mM sodium phosphate, pH 7.4, 5 mM DTT, 50mM ammonium sulfate, 5 µM pyroxidal 5 phosphate, 0.5 mM 3-acetyl pyridine adenine dinucleotide, 0.5 mM a-ketoglutarate, 5 mM leucine, 12.5 mM EDTA, 10 units/ml leucine dehydrogenase, and 10 nM human branch-chained aminotransferase-2 at 30C for 30 min.
Enzyme activation: Maximal activity of human branch-chained aminotransferase-2 requires pretreatment of enzyme with 100 mM final DTT for at least 1 hour at 4oC.
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