Recombinant Human BCAT2 protein

**Background of BCAT2 Recombinant Protein**

Branched-chain amino acid transaminase 2 (BCAT2) is a mitochondrial enzyme encoded by the *BCAT2* gene, playing a critical role in the metabolism of branched-chain amino acids (BCAAs: leucine, isoleucine, valine). It catalyzes the reversible transamination of BCAAs to their corresponding α-keto acids, linking amino acid catabolism to the tricarboxylic acid (TCA) cycle. BCAT2 is primarily expressed in peripheral tissues, such as the liver, skeletal muscle, and kidneys, where it regulates BCAA homeostasis and contributes to energy production, nitrogen shuttling, and gluconeogenesis.

Recombinant BCAT2 protein is engineered through molecular cloning and heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, functional enzyme for research applications. Its recombinant form retains catalytic activity, enabling studies on BCAA metabolism, enzyme kinetics, and interactions with substrates or inhibitors. BCAT2 has gained attention in metabolic disorders, cancer, and neurodegenerative diseases. For instance, dysregulated BCAA metabolism linked to BCAT2 activity is implicated in insulin resistance, obesity, and type 2 diabetes. In cancer, BCAT2 supports tumor growth by fueling the TCA cycle and promoting mTORC1 signaling via leucine-mediated activation.

Additionally, BCAT2’s role in neurotransmitter synthesis (e.g., glutamate) ties it to neurological conditions. Recombinant BCAT2 serves as a tool for drug discovery, structural analysis (e.g., X-ray crystallography), and elucidating metabolic adaptations in disease models. Challenges in studying endogenous BCAT2. such as tissue-specific isoforms and post-translational modifications, highlight the utility of recombinant protein in controlled experimental settings. Ongoing research aims to explore BCAT2 as a therapeutic target or biomarker in metabolic and oncological contexts.