BCAT1 Protein, Human (His, StrepⅡ)

The BCAT1 protein plays a key role in cellular processes as it catalyzes the initial reactions in the catabolism of the essential branched-chain amino acids leucine, isoleucine, and valine. This enzyme activity is essential for the breakdown of these amino acids, contributing to metabolic pathways necessary for energy production and nitrogen balance. BCAT1 Protein, Human (His, Strep) is the recombinant human-derived BCAT1 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

BCAT1 (Branched-chain amino acid transaminase 1) is an enzyme that catalyzes the initial reaction in the catabolism of the essential branched-chain amino acids leucine, isoleucine, and valine. This key step involves the reversible transamination of these amino acids, converting them into their respective branched-chain alpha-keto acids. BCAT1's enzymatic activity is crucial for regulating the levels of branched-chain amino acids and their metabolites, which play essential roles in various physiological processes, including energy metabolism and protein synthesis. It has to succinctly outline BCAT1's central role in the early stages of branched-chain amino acid catabolism, emphasizing its significance in maintaining amino acid homeostasis and supporting vital cellular functions.

Human

E. coli

N-StrepⅡ;N-6*His

P54687 (K2-S386)

586

Partial

KDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.