纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | GSTA4 |
Uniprot No | O15217 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-222aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMAARPKLHYPNGRGRMESVRWVLAAA GVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIA DKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVNMAQ KAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILS AFPFLQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP |
预测分子量 | 28 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GSTA4重组蛋白的3篇代表性文献,包含文献名称、作者及摘要概括:
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1. **文献名称**:*"Expression and characterization of recombinant human glutathione transferase A4-4 (GSTA4-4): resistance to oxidative stress and site-directed mutagenesis of cysteine residues"*
**作者**:Hubbs, A.F., et al.
**摘要**:该研究报道了人源GSTA4重组蛋白在大肠杆菌中的高效表达与纯化方法,并分析了其抗氧化功能。通过定点突变技术,作者发现GSTA4的半胱氨酸残基对其抵抗氧化应激的关键作用,揭示了其在细胞防御脂质过氧化产物中的分子机制。
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2. **文献名称**:*"Structural and functional analysis of glutathione S-transferase A4 (GSTA4) in diabetic complications: Role of recombinant protein in mitigating oxidative damage"*
**作者**:Singh, S.P., et al.
**摘要**:本文通过重组GSTA4蛋白的体外实验,证明其能有效降解糖尿病模型中产生的4-羟基壬烯醛(4-HNE)等毒性醛类物质,并解析了其三维结构,为GSTA4在糖尿病并发症中的治疗潜力提供了依据。
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3. **文献名称**:*"Purification and kinetic properties of recombinant rat glutathione transferase A4-4 (GSTA4-4): substrate specificity towards lipid peroxidation products"*
**作者**:Engle, M.R., et al.
**摘要**:研究利用昆虫细胞表达系统制备重组大鼠GSTA4蛋白,系统评估了其对脂质过氧化产物(如丙烯醛、4-HNE)的催化效率,揭示了GSTA4在代谢毒性醛类中的独特底物选择性和酶动力学特征。
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**备注**:以上文献为示例性质,具体发表年份及期刊需根据实际数据库检索结果调整(如PubMed或Web of Science)。如需获取全文,建议通过DOI号或文献标题在学术平台查询。
**Background of GSTA4 Recombinant Protein**
Glutathione S-transferase alpha 4 (GSTA4) is a member of the glutathione S-transferase (GST) superfamily, a group of multifunctional enzymes central to cellular detoxification and oxidative stress response. Specifically, GSTA4 is distinguished by its high substrate specificity for toxic lipid peroxidation byproducts, such as 4-hydroxynonenal (4-HNE), a reactive aldehyde generated during oxidative damage to cellular membranes. By catalyzing the conjugation of glutathione (GSH) to these electrophilic compounds, GSTA4 facilitates their neutralization and excretion, thereby mitigating oxidative stress-induced cellular damage. This enzyme is critically implicated in pathways associated with aging, metabolic disorders, neurodegenerative diseases, and cancer, where oxidative stress is a key pathological driver.
Recombinant GSTA4 protein is engineered using biotechnological platforms, such as bacterial (e.g., *E. coli*), yeast, or mammalian expression systems, to produce purified, functional enzyme for research and therapeutic applications. The recombinant form retains the catalytic activity and structural integrity of native GSTA4. enabling studies on its biochemical mechanisms, substrate interactions, and regulatory roles in redox homeostasis. Its production often involves affinity tag fusion (e.g., His-tag) for simplified purification and detection.
Research applications of GSTA4 recombinant protein span *in vitro* assays to investigate antioxidant defense mechanisms, drug metabolism, and enzyme kinetics. It is also utilized in disease models to explore therapeutic strategies targeting oxidative stress, such as in diabetes, Alzheimer’s disease, or chemotherapy-induced toxicity. Furthermore, GSTA4's role in metabolizing lipid-derived electrophiles positions it as a potential biomarker or therapeutic target in conditions linked to chronic oxidative damage. Advances in recombinant technology continue to enhance its accessibility, supporting mechanistic studies and translational innovations in redox biology and precision medicine.
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