| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TXNL4A |
| Uniprot No | P83876 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSYMLP HLHNGWQVDQ AILSEEDRVV VIRFGHDWDP TCMKMDEVLY SIAEKVKNFA VIYLVDITEV PDFNKMYELY DPCTVMFFFR NKHIMIDLGT GNNNKINWAM EDKQEMVDII ETVYRGARKG RGLVVSPKDY STKYRY |
| 预测分子量 | 19 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TXNL4A重组蛋白的3篇代表性文献概览(内容基于公开研究总结，非真实文献)：
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1. **标题**：*Structural insights into the redox regulation of TXNL4A and its interaction with the spliceosome*
**作者**：Chen L, et al.
**摘要**：本研究解析了重组TXNL4A蛋白的晶体结构，揭示了其硫氧还蛋白结构域中关键半胱氨酸残基在氧化还原调控中的作用，并发现其通过与剪接体核心组分USP39的相互作用参与RNA剪接过程。
2. **标题**：*TXNL4A knockdown induces oxidative stress and apoptosis in colorectal cancer cells*
**作者**：Wang Y, et al.
**摘要**：通过重组TXNL4A蛋白功能实验，发现其在结直肠癌细胞中通过调节ROS水平影响细胞凋亡，提示TXNL4A可能作为癌症治疗的潜在靶点。
3. **标题**：*Recombinant TXNL4A enhances DNA repair via modulating PRDX1 activity in radiation-resistant cells*
**作者**：Kumar S, et al.
**摘要**：利用重组TXNL4A蛋白验证其与过氧化物还原酶PRDX1的功能互作，证明其在电离辐射后通过修复氧化损伤的DNA维持基因组稳定性。
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如需获取真实文献，建议在PubMed或Web of Science中检索关键词：**TXNL4A recombinant protein**、**TXNL4A structure/function**。
**Background of TXNL4A Recombinant Protein**
TXNL4A (thioredoxin-like 4A), also known as DIM1. is a member of the thioredoxin protein family, characterized by a conserved thioredoxin-fold domain involved in redox regulation. This protein plays a critical role in RNA splicing and genomic stability. It functions as a core component of the U5 small nuclear ribonucleoprotein (snRNP) complex within the spliceosome, facilitating the removal of introns during mRNA processing. TXNL4A interacts with other splicing factors, such as the Survival of Motor Neuron (SMN) complex, to ensure proper assembly and recycling of spliceosomal components.
Recombinant TXNL4A is engineered through molecular cloning, typically expressed in *E. coli* or mammalian cell systems, to produce a purified, bioactive form for research. Its structure includes a redox-active CXXC motif, enabling disulfide reductase activity, though its primary role in splicing is redox-independent. Studies highlight its involvement in maintaining spliceosome integrity and regulating alternative splicing events linked to cellular stress responses, DNA repair, and cell cycle control.
Dysregulation of TXNL4A is associated with diseases, including spinal muscular atrophy (SMA) and cancer. In SMA, reduced SMN complex levels impair TXNL4A integration into snRNPs, disrupting splicing. In cancer, aberrant TXNL4A expression correlates with tumor progression and therapy resistance, potentially due to impaired DNA repair mechanisms. Recombinant TXNL4A serves as a tool to study splicing mechanisms, screen for splicing-targeted therapeutics, and explore its redox signaling roles. Its dual functionality in redox regulation and RNA processing makes it a unique candidate for understanding cellular homeostasis and disease pathogenesis.
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