| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HLA-G |
| Uniprot No | P17693 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-338aa |
| 氨基酸序列 | DAAQPARRAVRSLHHHHHHHHHHLVPRGSRTGSHSMRYFSAAVSRPGRGE PRFIAMGYVDDTQFVRFDSDSACPRMEPRAPWVEQEGPEYWEEETRNTKA HAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLLRGYEQYAYD GKDYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLH RYLENGKEMLQRADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQR DGEDQTQDVELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEP LMLRWKQSSLPTIPIMGIVAGLVVLAAVVTGAAVAAVLWRKKSSD |
| 预测分子量 | 40 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篇关于HLA-G重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*"HLA-G: A Human Placental Immunosuppressive Protein"*
**作者**：Rouas-Freiss, N., et al.
**摘要**：该研究阐述了重组HLA-G蛋白在体外实验中的免疫抑制功能，证明其通过结合NK细胞和T细胞受体抑制免疫反应，为妊娠期间母胎免疫耐受机制提供分子基础。
2. **文献名称**：*"Production of soluble HLA-G in prokaryotic and eukaryotic expression systems"*
**作者**：Park, G.M., et al.
**摘要**：比较了原核(大肠杆菌)和真核(哺乳动物细胞)系统表达重组HLA-G蛋白的优缺点，发现真核系统产生的蛋白更接近天然构象，适用于功能性研究。
3. **文献名称**：*"HLA-G structure and function in immune tolerance"*
**作者**：LeMaoult, J., et al.
**摘要**：通过重组HLA-G蛋白解析其结构与免疫调节功能的关联，揭示其β2-微球蛋白结合域对抑制树突状细胞成熟的关键作用，为肿瘤免疫逃逸研究提供依据。
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(注：以上文献信息为简化示例，实际引用需核对具体期刊及年份。)
Human leukocyte antigen-G (HLA-G) is a non-classical MHC class I molecule with unique immunomodulatory properties, primarily involved in maintaining immune tolerance. Unlike classical HLA class I proteins, HLA-G exhibits limited polymorphism and restricted tissue expression, predominantly in immune-privileged sites like the placenta, thymus, and certain tumors. It interacts with inhibitory receptors such as KIR2DL4 on natural killer (NK) cells and LILRB1/2 on myeloid cells, suppressing cytotoxic responses and promoting immune tolerance. This mechanism is critical in pregnancy, where HLA-G mediates maternal-fetal tolerance by protecting semi-allogeneic fetal tissues from maternal immune rejection. In pathological contexts, many cancers exploit HLA-G overexpression to evade immune surveillance, correlating with poor prognosis and metastasis.
Recombinant HLA-G proteins are artificially produced using genetic engineering, often in mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper glycosylation and structural integrity. These proteins retain functional epitopes for receptor binding and are used as research tools to study HLA-G-mediated immune regulation, develop diagnostic assays, or explore therapeutic applications. For instance, soluble HLA-G isoforms (e.g., HLA-G1 or HLA-G5) are investigated for their potential to mitigate graft rejection in transplantation or to treat autoimmune disorders by inducing tolerance. Challenges include maintaining post-translational modifications critical for receptor interactions and addressing variability in isoform-specific functions. Current research focuses on optimizing recombinant HLA-G production and elucidating its pleiotropic roles in immune evasion and tolerance, with implications for cancer immunotherapy and reproductive health.
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