Analytical Data
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Gene name
BCAT2
- Application
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Alternative Names
BCAT2；BCATM；BCT2；ECA40；Branched-chain-amino-acid aminotransferase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15382
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Expression Region
28-392aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMASSSFKAADLQLEMTQKPHKKPGPG EPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLF EGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLI EVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFP GGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQV LWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLL DMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILY KDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV
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Molecular Weight
44 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
BCAT2, or Branched-Chain Amino Acid Transaminase 2, is a crucial enzyme involved in the metabolism of branched-chain amino acids (BCAAs) such as leucine, isoleucine, and valine, which play significant roles in various physiological processes, including protein synthesis, energy production, and neurotransmitter regulation. Research on BCAT2 has gained prominence due to its potential implications in metabolic disorders, neurodegenerative diseases, and cancer. The enzyme exists in two isoforms, with BCAT2 primarily located in the mitochondria, while its counterpart, BCAT1, is found in the cytoplasm. Understanding the structure and function of BCAT2 is essential for deciphering its role in amino acid homeostasis and energy metabolism. Moreover, BCAT2 has been linked to conditions such as insulin resistance and diabetes, making it a significant target for therapeutic interventions. Recent studies have focused on the biochemical characterization of recombinant BCAT2, which involves expressing the protein in various systems to study its enzymatic activity, substrate specificity, and structural properties. These investigations aid in elucidating the enzyme's mechanism of action and its regulatory pathways, thereby paving the way for advanced research in metabolic therapies. The development of BCAT2 inhibitors or modulators could lead to novel strategies for treating metabolic syndromes, highlighting the importance of this enzyme in health and disease contexts. As the research landscape continues to evolve, the examination of BCAT2 not only enhances our understanding of amino acid metabolism but also contributes to the broader field of metabolic health and disease management, underscoring its importance in clinical and therapeutic research.
