| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | T273A |
| Uniprot No | P04133 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 133-324aa(T273A) |
| 氨基酸序列 | CEWDEAATALEINLEEEDDDNEDEVDEQAEQQKTHVFGQAPYSGINITKEGIQIGVEGQTPKYADKTFQPEPQIGESQWYETEINHAAGRVLKKTTPMKPCYGSYAKPTNENGGQGILVKQQNGKLESQVEMQFFSTTEAAAGNGDNLTPKVVLYSEDVDIETPDTHISYMPTIKEGNSRELMGQQSMPNRP |
| 预测分子量 | 50.3 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T273A重组蛋白的模拟参考文献示例(注：文献为虚构示例，仅供格式参考)：
1. **文献名称**：Structural and Functional Analysis of T273A Mutant Recombinant Protein in Cancer Signaling
**作者**：Zhang L., et al.
**摘要**：研究T273A突变对重组蛋白结构稳定性的影响，发现该突变通过破坏磷酸化位点抑制下游NF-κB信号通路，为靶向癌症治疗提供新机制。
2. **文献名称**：T273A Recombinant Protein Enhances Neuronal Survival in Alzheimer’s Disease Models
**作者**：Kim S., Patel R.
**摘要**：通过体外神经元模型证明，T273A重组蛋白通过降低tau蛋白异常磷酸化，显著减少淀粉样斑块沉积，延缓阿尔茨海默病病理进展。
3. **文献名称**：Kinetic Characterization of T273A-Modified Recombinant Enzyme in Metabolic Regulation
**作者**：Gupta A., et al.
**摘要**：利用酶动力学分析发现，T273A突变使重组蛋白对ATP的亲和力下降50%，揭示了其在代谢性疾病中能量感应功能的关键作用。
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**说明**：以上内容基于常见蛋白突变研究方向模拟生成，实际文献需通过PubMed/ScienceDirect等平台检索关键词(如"T273A recombinant protein"+"mutation")。若需真实文献，可提供具体蛋白名称(如p53-T273A、AKT1-T273A等)辅助精准查询。
**Background of T273A Recombinant Protein**
The T273A recombinant protein is a genetically engineered variant in which the threonine residue at position 273 is substituted with alanine. This site-specific mutation is often introduced to investigate the functional or structural role of post-translational modifications, particularly phosphorylation, as threonine residues are common targets for kinases. The T273A mutation disrupts the native phosphorylation site, enabling researchers to study its impact on protein activity, stability, or interaction with downstream signaling molecules.
Such recombinant proteins are widely utilized in biochemical and cellular studies to dissect signaling pathways, enzyme mechanisms, or disease-related processes. For example, in cancer research, T273A mutants may be employed to explore kinase-driven pathways (e.g., MAPK or PI3K/AKT) where phosphorylation at specific residues regulates cell proliferation, apoptosis, or metastasis. The mutation helps distinguish between constitutive activation and regulation-dependent behavior of the protein.
Production typically involves expression in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells), followed by purification via affinity tags (e.g., His-tag). The recombinant protein’s functionality is validated through assays such as kinase activity tests, binding studies, or cellular phenotypic analyses.
The T273A variant also serves as a tool for drug discovery, enabling screening of inhibitors targeting phosphorylation-dependent interactions. Its application extends to structural biology, where the mutation aids in crystallographic studies by stabilizing conformational states or eliminating heterogeneity caused by dynamic modifications.
Overall, the T273A recombinant protein exemplifies a precision tool for unraveling molecular mechanisms, bridging genetic engineering with functional proteomics to advance therapeutic and diagnostic innovations.
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