The branched-chain amino acid transaminase 1 (BCAT1) is a key enzyme in the metabolism of branched-chain amino acids (BCAAs: leucine, isoleucine, valine), catalyzing their conversion into corresponding α-keto acids. It plays a critical role in nitrogen homeostasis, neurotransmitter synthesis (e.g., glutamate), and cellular energy production. BCAT1 is highly expressed in the brain, skeletal muscle, and certain cancers, where its activity is linked to tumor progression, metabolic reprogramming, and resistance to therapies. Dysregulation of BCAT1 has been implicated in neurological disorders (e.g., Alzheimer’s disease, epilepsy) and cancers (e.g., gliomas, leukemias), making it a potential therapeutic or diagnostic target.
BCAT1 antibodies are essential tools for studying its expression, localization, and function. They are widely used in techniques like Western blot, immunohistochemistry, and immunofluorescence to assess BCAT1 levels in tissues or cultured cells. High-quality BCAT1 antibodies are validated for specificity, often using knockout cell lines or siRNA knockdown controls. Researchers also employ these antibodies to explore BCAT1’s role in metabolic pathways, its interaction with signaling molecules like mTOR, and its impact on cancer cell proliferation or neuronal survival. Commercial availability of BCAT1 antibodies from multiple vendors facilitates broad research applications, though variability in antibody performance necessitates careful validation for experimental consistency.