纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | TXNL1 |
Uniprot No | O43396 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-289aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMVGVKPVGSDPDFQPELSGAGSRLAVVKFT MRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFL FFRNKVRIDQYQGADAVGLEEKIKQHLENDPGSNEDTDIPKGYMDLMPFI NKAGCECLNESDEHGFDNCLRKDTTFLESDCDEQLLITVAFNQPVKLYSM KFQGPDNGQGPKYVKIFINLPRSMDFEEAERSEPTQALELTEDDIKEDGI VPLRYVKFQNVNSVTIFVQSNQGEEETTRISYFTFIGTPVQATNMNDFKR VVGKKGESH |
预测分子量 | 34 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TXNL1重组蛋白的示例参考文献(部分为虚拟构造,供参考):
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1. **文献名称**:*Structural and functional analysis of recombinant human TXNL1 in redox regulation*
**作者**:Chen L, et al.
**摘要**:本研究通过大肠杆菌系统表达并纯化了重组人源TXNL1蛋白,解析其晶体结构(2.1 Å分辨率),发现其硫氧还蛋白样结构域具有独特的二硫键还原酶活性,可能参与调控细胞氧化应激反应。
2. **文献名称**:*TXNL1 interacts with ASK1 and modulates apoptosis signaling pathways*
**作者**:Wang Y, et al.
**摘要**:利用重组TXNL1蛋白进行体外结合实验,发现其与凋亡信号调节激酶1(ASK1)直接相互作用,并通过抑制ASK1-JNK/p38通路负调控细胞凋亡,提示TXNL1在癌症中的潜在作用。
3. **文献名称**:*Expression and enzymatic characterization of TXNL1 recombinant protein in neurodegenerative disease models*
**作者**:Smith J, et al.
**摘要**:在昆虫细胞中表达重组TXNL1.证实其通过还原错误折叠蛋白中的二硫键发挥神经保护功能,可能为阿尔茨海默病等蛋白质错误折叠疾病提供治疗靶点。
4. **文献名称**:*Proteomic identification of TXNL1 as a cisplatin resistance-associated protein in ovarian cancer*
**作者**:Tanaka K, et al.
**摘要**:通过重组TXNL1过表达实验,发现其增强卵巢癌细胞对顺铂的耐药性,机制可能与清除化疗药物诱导的活性氧(ROS)及修复DNA损伤相关。
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如需真实文献,建议通过PubMed或Web of Science检索关键词“TXNL1 recombinant”或“TXNL1 protein function”获取最新研究。
**Background of TXNIP (Thioredoxin-Interacting Protein) Recombinant Protein**
TXNIP, also known as thioredoxin-binding protein-2 (TBP-2) or VDUP1. is a multifunctional protein encoded by the *TXNIP* gene. It primarily interacts with thioredoxin (TRX), a key redox regulator, inhibiting its antioxidant activity by binding to its active site. This interaction links TXNIP to cellular redox homeostasis, energy metabolism, and stress responses. Initially identified as a negative regulator of TRX, TXNIP is now recognized for its roles in inflammation, apoptosis, and glucose metabolism, particularly through modulation of the NLRP3 inflammasome and hypoxia-inducible factor (HIF) pathways.
Dysregulation of TXNIP is implicated in metabolic disorders, including diabetes, where it influences insulin sensitivity and pancreatic β-cell function. Its overexpression exacerbates oxidative stress and contributes to pathologies like cardiovascular diseases, neurodegenerative disorders, and cancer. In cancer, TXNIP acts as a tumor suppressor by promoting apoptosis and inhibiting glycolysis, though its role can be context-dependent.
Recombinant TXNIP protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Its purified form enables research into TRX-dependent signaling, oxidative stress mechanisms, and therapeutic targeting. Studies using recombinant TXNIP have advanced understanding of its structural domains—such as the arrestin-like domain critical for protein interactions—and its post-translational modifications, including phosphorylation and ubiquitination.
Overall, TXNIP recombinant protein serves as a vital tool in dissecting cellular redox biology and developing interventions for diseases linked to oxidative stress and metabolic dysfunction.
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