| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HLA-A |
| Uniprot No | P30443 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-308aa |
| 氨基酸序列 | GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYLEGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPI |
| 预测分子量 | 38.3 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. |
以下为模拟生成的3-4条关于HLA-A重组蛋白的参考文献(非真实存在，仅作格式示例)：
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1. **文献名称**: "Structural analysis of recombinant HLA-A*02:01 complexed with viral peptide"
**作者**: Smith J, et al.
**摘要**: 通过X射线晶体学解析HLA-A*02:01重组蛋白与流感病毒肽段的复合物结构，揭示了抗原结合域的关键相互作用，为疫苗设计提供结构基础。
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2. **文献名称**: "High-yield expression of soluble HLA-A in HEK293 cells using codon optimization"
**作者**: Chen L, Wang Y.
**摘要**: 通过密码子优化和哺乳动物细胞表达系统(HEK293)实现HLA-A重组蛋白的高效可溶性表达，产量提升3倍，适用于大规模抗原呈递研究。
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3. **文献名称**: "HLA-A recombinant proteins in cancer immunotherapy: TCR binding affinity screening"
**作者**: Gonzalez R, et al.
**摘要**: 利用重组HLA-A蛋白筛选肿瘤相关抗原肽与T细胞受体(TCR)的结合亲和力，鉴定出多个高亲和力候选分子，推动个体化免疫疗法开发。
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4. **文献名称**: "Comparative analysis of HLA-A allelic variants in autoimmune disease models"
**作者**: Tanaka K, et al.
**摘要**: 对比6种HLA-A重组蛋白在类风湿性关节炎模型中的抗原呈递差异，发现HLA-A*01:01变异体显著增强自身免疫反应，提示特定亚型在疾病中的功能特异性。
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提示：实际文献需通过PubMed/Google Scholar检索关键词如“recombinant HLA-A protein”或“HLA-A expression and purification”，并结合具体研究领域(结构、免疫、疾病等)筛选。
HLA-A recombinant protein is a genetically engineered variant of the human leukocyte antigen class A (HLA-A), a critical component of the major histocompatibility complex (MHC) class I system in humans. HLA molecules play a central role in adaptive immunity by presenting peptide antigens to CD8+ T cells, enabling immune surveillance against infected or malignant cells. The HLA-A locus is highly polymorphic, with numerous allelic variants influencing antigen-binding specificity and immune responses. This genetic diversity complicates studies of HLA-associated diseases, vaccine development, and personalized immunotherapies.
Recombinant HLA-A proteins are typically produced using expression systems like *E. coli*, insect cells, or mammalian cells to ensure proper folding and post-translational modifications. These proteins often consist of the HLA-A heavy chain (α subunit) non-covalently linked to β2-microglobulin, forming a stable heterodimer. The antigen-binding groove can be loaded with synthetic or pathogen-derived peptides for functional studies.
Such recombinant proteins are indispensable tools in immunological research. They facilitate T cell receptor (TCR) specificity profiling, vaccine efficacy testing, and mechanistic studies of autoimmune disorders, infectious diseases, and cancer immunotherapy. For example, HLA-A-peptide tetramers generated from recombinant proteins enable precise detection of antigen-specific T cells. Additionally, structural studies using X-ray crystallography or cryo-EM rely on purified HLA-A complexes to elucidate peptide-MHC interactions.
Recent advancements in recombinant technology have enhanced the scalability and customization of HLA-A proteins, supporting high-throughput screening for neoantigen discovery and TCR-based therapies. Their application continues to drive innovations in precision medicine and our understanding of immune regulation.
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