| 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篇参考文献示例(注：文献为虚拟示例，实际引用需查询具体数据库)：
1. **"Production and functional characterization of recombinant ULBP1 for NK cell activation studies"**
- 作者：Smith A, et al.
- 摘要：研究报道了通过哺乳动物表达系统成功表达并纯化ULBP1重组蛋白，证实其能够有效结合NKG2D受体，并增强自然杀伤(NK)细胞对肿瘤细胞的杀伤活性。
2. **"Structural insights into ULBP1-NKG2D interaction using recombinant protein crystallography"**
- 作者：Zhang L, et al.
- 摘要：通过重组ULBP1蛋白的晶体结构解析，揭示了其与NKG2D受体的结合界面关键氨基酸残基，为设计基于ULBP1的免疫治疗策略提供结构基础。
3. **"Recombinant ULBP1 enhances antitumor immunity in a murine melanoma model"**
- 作者：Johnson R, et al.
- 摘要：在小鼠黑色素瘤模型中，重组ULBP1蛋白联合检查点抑制剂显著提高CD8+ T细胞浸润和肿瘤消退，表明其在癌症免疫治疗中的潜在应用价值。
如需真实文献，建议在PubMed或Web of Science中检索关键词“recombinant ULBP1”或“ULBP1 protein”。
ULBP1 (UL16-binding protein 1) is a cell surface glycoprotein belonging to the human NKG2D ligand family, which includes MHC class I chain-related (MIC) and RAET1/ULBP proteins. It plays a critical role in innate and adaptive immune responses by interacting with the NKG2D receptor expressed on natural killer (NK) cells, γδ T cells, and CD8+ αβ T cells. This interaction triggers cytotoxic activity against infected, stressed, or malignant cells, making ULBP1 a key mediator of immune surveillance.
Structurally, ULBP1 is a type I transmembrane protein with an extracellular α1/α2 domain fold resembling MHC class I molecules, though it lacks the α3 domain and does not associate with β2-microglobulin. Its expression is typically low in healthy tissues but upregulated under cellular stress, viral infection, or DNA damage. Many cancers, including leukemia, melanoma, and solid tumors, overexpress ULBP1 as a result of oncogenic stress, making it a potential biomarker and therapeutic target.
Recombinant ULBP1 proteins are engineered using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper glycosylation and structural integrity. These proteins retain the functional NKG2D-binding domain and are purified through affinity chromatography for research applications. They are widely used to study NKG2D-mediated immune activation mechanisms, screen therapeutic antibodies, and develop cancer immunotherapies such as bispecific antibodies or CAR-T cells targeting the ULBP1-NKG2D axis. Additionally, soluble ULBP1 variants serve as decoy receptors to modulate immune responses in autoimmune diseases. The development of ULBP1-based recombinant proteins continues to advance our understanding of tumor immunology and therapeutic intervention strategies.
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