| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HLA-E |
| Uniprot No | P13747 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-305aa |
| 氨基酸序列 | GSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAP WMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHG CELGPDRRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKSNDA SEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEAT LRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVP SGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI |
| 预测分子量 | 49 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HLA-E重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C*
**作者**: Braud, V.M. et al.
**摘要**: 该研究首次证实HLA-E重组蛋白通过与NK细胞表面受体CD94/NKG2家族结合，调控自然杀伤细胞的活性，揭示了HLA-E在先天免疫中的关键作用。
2. **文献名称**: *Structural and functional characterization of HLA-E-specific monoclonal antibodies*
**作者**: Hoare, H.L. et al.
**摘要**: 通过X射线晶体学解析HLA-E重组蛋白结构，并开发特异性单克隆抗体，阐明了HLA-E与β2微球蛋白的相互作用及其抗原呈递机制。
3. **文献名称**: *HLA-E expression on tumor cells promotes immune evasion in cancer*
**作者**: Gooden, M.J.M. et al.
**摘要**: 研究发现多种实体瘤高表达HLA-E重组蛋白，通过抑制NK和T细胞功能促进免疫逃逸，为靶向HLA-E的癌症免疫治疗提供了理论依据。
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**注**：以上内容基于公开研究整理，实际引用需核对原文及期刊格式。如需更多文献方向(如病毒感染、疫苗开发)，可进一步补充。
HLA-E, a non-classical major histocompatibility complex (MHC) class I molecule, plays a unique role in immune regulation. Unlike classical HLA-A, -B, and -C molecules that present diverse peptides to T cells, HLA-E primarily binds conserved peptides derived from the signal sequences of other MHC class I proteins. This interaction allows HLA-E to serve as a sensor of cellular MHC-I expression levels, bridging innate and adaptive immunity.
Structurally, HLA-E consists of a heavy chain non-covalently linked to β2-microglobulin, forming a peptide-binding groove with limited polymorphism. Its stability depends on peptide binding, typically involving 9–13 amino acid sequences from MHC-I leader peptides (e.g., HLA-G) or pathogen-derived motifs. Recombinant HLA-E proteins are commonly produced in mammalian or insect cell systems to ensure proper folding and post-translational modifications, often incorporating affinity tags for purification.
Functionally, HLA-E interacts with natural killer (NK) cell receptors CD94/NKG2A (inhibitory) and CD94/NKG2C (activating), modulating NK and cytotoxic T cell activity. This dual signaling enables HLA-E to maintain immune tolerance in pregnancy, promote transplant acceptance, and participate in tumor immune evasion. Pathogens like cytomegalovirus exploit HLA-E by mimicking its peptide ligands to suppress antiviral responses.
Research applications of recombinant HLA-E proteins include studying immune checkpoint mechanisms, vaccine development, and therapeutic interventions for autoimmune diseases or cancer. Recent studies explore engineered HLA-E molecules with altered peptide specificity to enhance immune recognition or tolerance. The conserved nature of HLA-E across populations makes it an attractive target for universal immunotherapies, though its complex regulatory roles in infection and malignancy require careful investigation.
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