| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ULBP1 |
| Uniprot No | Q9BZM6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-216aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMGWVDT HCLCYDFIIT PKSRPEPQWC EVQGLVDERP FLHYDCVNHK AKAFASLGKK VNVTKTWEEQ TETLRDVVDF LKGQLLDIQV ENLIPIEPLT LQARMSCEHE AHGHGRGSWQ FLFNGQKFLL FDSNNRKWTA LHPGAKKMTE KWEKNRDVTM FFQKISLGDC KMWLEEFLMY WEQMLDPTKP PSLAPG |
| 预测分子量 | 25 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ULBP1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"ULBP1 is a non-native NKG2D ligand for HCMV-specific CD8+ T cell recognition"*
**作者**：Rölle A, et al.
**摘要**：该研究探讨了ULBP1作为NKG2D非经典配体在人类巨细胞病毒(HCMV)感染中的作用，通过重组ULBP1蛋白验证其与病毒特异性CD8+ T细胞的相互作用，揭示了其在免疫逃逸中的潜在机制。
2. **文献名称**：*"Expression of NKG2D ligands and binding of recombinant NKG2D-Fc fusion proteins to human tumour cell lines"*
**作者**：Eagle RA, et al.
**摘要**：研究利用重组NKG2D-Fc融合蛋白(包括ULBP1重组蛋白)分析其与多种肿瘤细胞系的结合能力，证实ULBP1在肿瘤细胞表面的异常表达可激活NK细胞抗肿瘤活性。
3. **文献名称**：*"Soluble NKG2D ligands in sera of cancer patients: release of ULBP1 from tumor cells by proteolytic cleavage"*
**作者**：Salih HR, et al.
**摘要**：通过重组ULBP1蛋白技术，研究发现肿瘤患者血清中可溶性ULBP1来源于肿瘤细胞表面的蛋白水解切割，这种可溶性形式可能抑制NK细胞介导的免疫监视。
4. **文献名称**：*"Molecular mechanisms of soluble ULBP1-mediated NK cell activation"*
**作者**：Chitadze G, et al.
**摘要**：研究利用重组可溶性ULBP1蛋白，揭示其通过结合NKG2D受体激活NK细胞信号通路的分子机制，为癌症免疫治疗提供新靶点。
(注：以上文献信息为模拟示例，实际引用需核对具体文献内容及发表细节。)
ULBP1 (UL16-binding protein 1), a member of the human NKG2D ligand family, plays a critical role in immune surveillance by activating natural killer (NK) cells and T lymphocytes through interaction with the NKG2D receptor. This stress-inducible glycoprotein is structurally related to MHC class I molecules but lacks the α3 domain and is anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) linkage. Its expression is typically low in healthy tissues but upregulated in infected, malignant, or otherwise stressed cells, marking them for immune recognition.
Recombinant ULBP1 protein is engineered through genetic modification to enable large-scale production, typically using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications. The recombinant form often retains the extracellular α1/α2 domains essential for NKG2D binding while omitting the GPI anchor, creating a soluble version. This modification enhances its utility in therapeutic and research applications by improving stability and reducing membrane-associated technical constraints.
In cancer immunotherapy, recombinant ULBP1 shows promise as a tool to enhance anti-tumor responses. It can be used to stimulate NKG2D-mediated cytotoxicity in vitro, develop chimeric antigen receptor (CAR) T-cells, or serve as a decoy ligand to inhibit tumor immune evasion mechanisms. Additionally, it serves as a critical reagent for studying NKG2D signaling pathways, ligand-receptor interactions, and tumor microenvironment dynamics. Pharmaceutical applications include its incorporation into bispecific antibodies and vaccine adjuvants designed to amplify immune recognition of malignancies. Quality-controlled batches are validated through functional assays like surface plasmon resonance and cytotoxicity tests to ensure biological activity.
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