| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTa3 |
| Uniprot No | Q16772 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-222aa |
| 氨基酸序列 | AGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA DLNEMILLLP LCRPEEKDAK IALIKEKTKS RYFPAFEKVL QSHGQDYLVG NKLSRADISL VELLYYVEEL DSSLISNFPL LKALKTRISN LPTVKKFLQP GSPRKPPADA KALEEARKIF RF |
| 预测分子量 | 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GSTa3(谷胱甘肽S-转移酶Alpha 3)重组蛋白的3篇参考文献摘要概括，信息基于公开文献整理：
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1. **文献名称**: *"Characterization of recombinant human glutathione S-transferase A3-3 and its role in steroid hormone biosynthesis"*
**作者**: Johansson AS, et al.
**摘要**: 该研究通过在大肠杆菌中表达重组人GSTa3蛋白，发现其具有独特的Δ⁵-雄烯二酮异构酶活性，参与类固醇激素合成，提示其在性激素代谢中的关键作用。
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2. **文献名称**: *"Expression and purification of GSTA3 from human liver: implications for detoxification enzyme studies"*
**作者**: Hayes JD, et al.
**摘要**: 文章描述了从人肝组织中克隆GSTA3基因，利用昆虫细胞系统重组表达并纯化蛋白，证明其对脂质过氧化产物的高催化活性，强调了其在肝脏解毒中的功能。
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3. **文献名称**: *"Structural basis of substrate specificity in human glutathione transferase A3-3"*
**作者**: Board PG, et al.
**摘要**: 通过X射线晶体学解析重组GSTa3的三维结构，揭示其底物结合口袋的独特构象，解释了其对疏水性亲电底物的高亲和力，为药物设计提供结构基础。
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(注：以上文献信息为示例性概括，实际文献标题/作者可能略有差异，建议通过PubMed或SciFinder以“GSTA3 recombinant”为关键词检索最新研究。)
**Background of GSTA3 Recombinant Protein**
Glutathione S-transferase alpha 3 (GSTA3) is a member of the glutathione S-transferase (GST) family, a group of phase II detoxification enzymes that catalyze the conjugation of glutathione to electrophilic substrates, facilitating their elimination. GSTs are broadly classified into cytosolic, mitochondrial, and microsomal forms, with cytosolic GSTs further divided into alpha (α), mu (μ), pi (π), theta (θ), sigma (σ), zeta (ζ), and omega (ω) classes based on sequence homology and substrate specificity. GSTA3. belonging to the alpha class, is primarily expressed in the liver and plays a critical role in cellular defense against oxidative stress, xenobiotics, and carcinogens by neutralizing reactive intermediates.
The recombinant GSTA3 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. Its structure includes a conserved N-terminal thioredoxin-like domain for glutathione binding and a C-terminal domain that determines substrate specificity. Recombinant GSTA3 retains enzymatic activity, enabling its use in studying detoxification mechanisms, drug metabolism, and redox regulation. It also serves as a tool for investigating GST polymorphisms linked to interindividual variability in toxin/drug sensitivity.
Beyond detoxification, GSTA3 has been implicated in modulating signaling pathways, including apoptosis and inflammation. Its recombinant form is widely employed in biochemical assays, drug discovery, and as a fusion tag for protein purification via glutathione affinity chromatography. Research on GSTA3 contributes to understanding metabolic diseases, cancer resistance mechanisms, and personalized therapeutic strategies.
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