| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | A143V |
| Uniprot No | P16710 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-377aa |
| 氨基酸序列 | MGAAVTLNRIKIAPGIADIRDKYMELGFNYPEYNRAVKFAEESYTYYYETSPGEIKPKFCLIDGMSIDHCSSFIVPEFAKQYVLIHGEPCSSFKFRPGSLIYYQNEVTPEYIKDLKHATDYIASGQRCHFIKKDYLLGDSDSVAKCCSKTNTKHCPKIFNNNYKTEHCDDFMTGFCRNDPGNPNCLEWLRAKRKPAMSTYSDICSKHMDARYCSEFIRIIRPDYFTFGDTALYVFCNDHKGNRNCWCANYPKSNSGDKYLGPRVCWLHECTDESRDRKWLYYNQDVQRTRCKYVGCTINVNSLALKNSQAELTSNCTRTTSAVGDVHPGEPVVKDKIKLPTWLGAAITLVVISVIFYFISIYSRPKIKTNDINVRRR |
| 预测分子量 | 43,4 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A143V重组蛋白的3篇参考文献示例(注：文献为模拟示例，实际研究中请根据具体数据库检索验证)：
1. **文献名称**: *"Impact of A143V Mutation on Recombinant HIV-1 Reverse Transcriptase Activity"*
**作者**: Smith J, et al.
**摘要**: 研究A143V突变对HIV-1重组逆转录酶功能的影响，发现该突变导致酶催化活性降低，并增强对非核苷类逆转录酶抑制剂(NNRTIs)的抗性。
2. **文献名称**: *"Structural and Functional Analysis of A143V Variant in Recombinant Cytochrome P450 2B6"*
**作者**: Lee S, et al.
**摘要**: 通过X射线晶体学分析A143V突变对细胞色素P450 2B6结构的影响，表明突变改变了底物结合口袋的构象，从而影响药物代谢效率。
3. **文献名称**: *"A143V Substitution in Recombinant Influenza A Virus Polymerase Affects Viral Replication"*
**作者**: Zhang Y, et al.
**摘要**: 探讨A143V突变在甲型流感病毒重组RNA聚合酶中的作用，发现该突变通过干扰聚合酶与病毒RNA的结合，显著降低病毒复制能力。
如需具体文献，建议在PubMed或Web of Science中检索关键词 **"A143V recombinant protein"** 或结合相关蛋白名称(如HIV RT、CYP450等)进行筛选。
The A143V recombinant protein is a genetically engineered variant of a naturally occurring protein, generated through site-directed mutagenesis to substitute alanine (A) with valine (V) at position 143. This single-nucleotide polymorphism (SNP) alters the protein's structural or functional properties, often linked to disease-associated pathways. The mutation is frequently studied in contexts such as neurodegenerative disorders (e.g., TDP-43 or SOD1 in ALS) or metabolic enzymes (e.g., GSTP1 in detoxification), where residue 143 may influence substrate binding, enzymatic activity, or protein aggregation. Recombinant expression systems (e.g., E. coli, HEK293 cells) are used to produce the mutant protein, enabling comparative studies with wild-type counterparts. Researchers analyze its biophysical traits (stability, folding), cellular localization, and interactions to decipher mechanistic roles in pathology. The A143V variant has also been explored in pharmacogenomics, as the mutation may affect drug efficacy or toxicity. Its study contributes to personalized medicine and targeted therapy development. Production typically involves affinity tags (e.g., His-tag) for purification, followed by functional validation via assays like Western blot, ELISA, or enzymatic activity tests. Current research focuses on elucidating how this subtle amino acid change drives molecular dysfunction, offering insights into disease mechanisms and therapeutic intervention strategies.
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