纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | TXNDC15 |
Uniprot No | Q96J42 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 33-321aa |
氨基酸序列 | VEVAEESGRLWSEEQPAHPLQVGAVYLGEEELLHDPMGQDRAAEEANAVL GLDTQGDHMVMLSVIPGEAEDKVSSEPSGVTCGAGGAEDSRCNVRESLFS LDGAGAHFPDREEEYYTEPEVAESDAAPTEDSNNTESLKSPKVNCEERNI TGLENFTLKILNMSQDLMDFLNPNGSDCTLVLFYTPWCRFSASLAPHFNS LPRAFPALHFLALDASQHSSLSTRFGTVAVPNILLFQGAKPMARFNHTDR TLETLKIFIFNQTGIEAKKNVVVTQADQIGPLPSTLIKSVDHHHHHH |
预测分子量 | 33 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TXNDC15重组蛋白的模拟参考文献示例(注:以下内容为假设性概括,实际文献需通过学术数据库核实):
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1. **文献名称**: *"Cloning and Functional Characterization of Recombinant TXNDC15 in Hepatocellular Carcinoma"*
**作者**: Li, X.; Wang, Y.; Chen, J.
**摘要**: 本研究成功在大肠杆菌系统中表达并纯化了重组TXNDC15蛋白,验证其硫氧还蛋白活性。实验表明,TXNDC15通过调节氧化应激通路抑制肝癌细胞增殖,提示其可能作为潜在治疗靶点。
2. **文献名称**: *"TXNDC15 Recombinant Protein Promotes Gastric Cancer Metastasis via ERK Signaling Pathway"*
**作者**: Kim, S.; Park, H.; Lee, D.
**摘要**: 通过哺乳动物细胞表达系统获得高纯度TXNDC15重组蛋白,发现其与胃癌细胞迁移相关。机制研究表明,TXNDC15通过激活ERK信号通路促进肿瘤侵袭,为胃癌预后提供了新生物标志物。
3. **文献名称**: *"Structural Analysis and Antioxidant Role of Recombinant TXNDC15 in Chronic Inflammation"*
**作者**: Smith, R.; Johnson, A.; Brown, K.
**摘要**: 解析了重组TXNDC15的晶体结构,揭示其硫氧还蛋白结构域的关键功能位点。功能实验显示,该蛋白通过清除活性氧(ROS)缓解慢性炎症模型中的组织损伤。
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**建议**:实际研究中请通过 **PubMed**(https://pubmed.ncbi.nlm.nih.gov)或 **Google Scholar** 检索最新文献,关键词可组合:TXNDC15 + recombinant protein/expression/function。
TXNDC15 (thioredoxin domain-containing protein 15) is a member of the thioredoxin superfamily, characterized by a conserved thioredoxin-like fold involved in redox regulation and disulfide bond formation. This endoplasmic reticulum (ER)-resident protein plays roles in protein folding, oxidative stress response, and modulation of ER stress pathways. It contains a signal peptide for ER localization and a C-terminal redox-active domain, though its enzymatic activity remains less defined compared to classical thioredoxins.
Research links TXNDC15 to cancer progression, particularly in esophageal squamous cell carcinoma, gastric cancer, and hepatocellular carcinoma, where its overexpression correlates with enhanced tumor cell proliferation, migration, and chemoresistance. Mechanistically, it may interact with ER chaperones (e.g., GRP78) or signaling pathways like PI3K/AKT to promote survival under stress.
Recombinant TXNDC15 protein is typically produced in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., HEK293 cells) with affinity tags (His, GST) for purification. Its applications include functional studies to dissect redox regulatory networks, ER stress-related disease mechanisms, and drug screening for cancer therapies. Structural analyses aim to clarify its substrate-binding motifs and redox-dependent interactions. Despite emerging pathological relevance, its physiological roles and precise molecular targets remain under investigation, highlighting the need for further biochemical and translational studies.
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