| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | MHCA |
| Uniprot No | P12844 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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3篇与MHC重组蛋白相关的模拟参考文献示例(内容为虚构，仅作格式参考)：
---
1. **文献名称**：*Efficient prokaryotic expression and purification of functional MHC class I molecules for T cell receptor binding assays*
**作者**：Zhang, L., et al.
**摘要**：本研究开发了一种基于大肠杆菌表达系统的重组MHC I类分子(HLA-A*02:01)高效生产方法，通过优化包涵体复性工艺获得可溶性蛋白，并验证其与抗原肽及T细胞受体的特异性结合能力，为免疫诊断试剂开发提供基础。
---
2. **文献名称**：*Structural insights into peptide-MHC complex stability using recombinant single-chain trimers*
**作者**：Smith, J.R., et al.
**摘要**：通过构建单链三聚体(包含β2微球蛋白、MHC重链和抗原肽)，解析了重组MHC-抗原复合物的晶体结构，揭示了关键氨基酸残基对复合物稳定性的影响，为疫苗设计中的表位优化提供结构生物学依据。
---
3. **文献名称**：*Application of MHC tetramers in tracking virus-specific CD8+ T cells during influenza infection*
**作者**：Tanaka, K., et al.
**摘要**：利用昆虫细胞表达系统制备重组MHC I类分子四聚体，结合流式细胞术定量分析流感病毒感染模型中的抗原特异性T细胞动态，证明该方法在评估免疫应答效能中的高灵敏度和特异性。
---
(注：如需真实文献，建议通过PubMed或Web of Science以关键词“recombinant MHC protein”或“MHC multimer”检索近年研究。)
**Background of MHC Class I-related Protein A (MHCA) Recombinant Protein**
MHC Class I-related protein A (MHCA), also known as MR1. is a non-classical major histocompatibility complex (MHC) molecule that plays a unique role in antigen presentation and immune regulation. Unlike classical MHC class I proteins, which present peptide antigens to T cells, MHCA is specialized in binding and presenting microbial metabolites, such as vitamin B derivatives, to mucosal-associated invariant T (MAIT) cells. This interaction is critical for bridging innate and adaptive immunity, particularly in detecting intracellular bacterial infections and coordinating early immune responses.
Recombinant MHCA proteins are engineered using biotechnological approaches, often involving the expression of codon-optimized MHCA genes in host systems like *E. coli* or mammalian cell lines. These proteins retain the structural and functional properties of native MHCA, including the ability to form stable complexes with antigenic ligands. Purification techniques such as affinity chromatography ensure high purity and bioactivity, making them valuable tools for immunological research.
In therapeutic contexts, recombinant MHCA proteins are explored for their potential in vaccine development, infectious disease modeling, and cancer immunotherapy. They enable the study of MAIT cell activation mechanisms, antigen-specific immune modulation, and the design of novel therapeutics targeting microbial-driven pathologies. Additionally, recombinant MHCA serves as a platform for structural studies, aiding in the elucidation of ligand-binding dynamics and receptor interactions.
Challenges in MHCA recombinant protein production include maintaining proper folding and post-translational modifications (e.g., glycosylation) critical for functionality. Advances in expression systems and bioprocessing continue to address these limitations, enhancing their applicability in both basic research and clinical innovation.
×
