| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | BCAT2 |
| Uniprot No | O15382 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-392aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMASSSFKAADLQLEMTQKPHKKPGPG EPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLF EGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLI EVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFP GGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQV LWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLL DMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILY KDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV |
| 预测分子量 | 44 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于BCAT2重组蛋白的3篇参考文献示例(注：文献为模拟示例，实际引用需根据真实文献调整)：
1. **文献名称**：*Expression and Purification of Recombinant Human BCAT2 in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究报道了人源BCAT2在大肠杆菌中的高效重组表达及纯化策略。通过优化表达条件和亲和层析技术，获得了高纯度且具有酶活性的BCAT2蛋白，为后续功能研究提供基础。
2. **文献名称**：*Structural Insights into BCAT2 Catalytic Mechanism via X-ray Crystallography*
**作者**：Johnson R, et al.
**摘要**：作者利用重组BCAT2蛋白进行X射线晶体学分析，解析了其三维结构，揭示了支链氨基酸底物结合的关键位点，并探讨了其转氨酶活性的分子机制。
3. **文献名称**：*BCAT2 Recombinant Protein as a Therapeutic Target in Cancer Metabolism*
**作者**：Lee S, et al.
**摘要**：该研究通过体外实验验证了重组BCAT2蛋白在癌细胞支链氨基酸代谢中的核心作用，并发现抑制其活性可显著降低肿瘤细胞增殖，提示其作为抗癌靶点的潜力。
如需具体文献，建议在PubMed或Web of Science中检索关键词“BCAT2 recombinant protein”或“BCAT2 expression”获取真实数据。
Branched-chain aminotransferase 2 (BCAT2) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme central to the metabolism of branched-chain amino acids (BCAAs: leucine, isoleucine, and valine). It catalyzes the reversible transamination of BCAAs, converting them into their corresponding α-keto acids while simultaneously generating glutamate. This reaction bridges BCAA catabolism with the tricarboxylic acid (TCA) cycle and nitrogen metabolism, playing a critical role in energy homeostasis and nitrogen balance. BCAT2 is primarily expressed in mitochondria of non-hepatic tissues, including skeletal muscle, kidneys, and the brain, contrasting with its cytosolic isoform, BCAT1. which is prevalent in the liver and nervous system.
Recombinant BCAT2 protein is produced using biotechnological platforms (e.g., E. coli or mammalian expression systems) to enable functional and structural studies. Its recombinant form retains enzymatic activity and PLP-binding capacity, making it invaluable for investigating BCAA dysregulation in metabolic disorders (e.g., diabetes, obesity) and neurological diseases. Notably, BCAT2 is implicated in cancer progression, as certain tumors exploit BCAA metabolism to fuel proliferation. Recombinant BCAT2 facilitates drug screening for inhibitors targeting BCAA-dependent pathways in oncology.
Structural studies using recombinant BCAT2 have elucidated substrate-binding mechanisms and regulatory sites, aiding the design of modulators. Additionally, it serves as a tool to explore BCAT2's role in mTORC1 signaling activation via leucine sensing. Challenges in recombinant production include maintaining proper folding and PLP incorporation, often addressed through codon optimization or chaperone co-expression. Ongoing research leverages recombinant BCAT2 to decode its tissue-specific roles and therapeutic potential in precision medicine.
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