| 纯度 | > 85 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD38 |
| Uniprot No | P28907 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 46-300aa |
| 氨基酸序列 | WRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI |
| 预测分子量 | 56.2 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CD38重组蛋白的3篇代表性文献，涵盖结构、功能及治疗应用研究：
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1. **文献名称**：*"Structural basis for enzymatic activity and protein-protein interactions of human CD38 in NAD+ metabolism"*
**作者**：Liu, Q., Kriksunov, I.A., Graeff, R., et al.
**摘要**：该研究通过X射线晶体学解析了人源CD38重组蛋白的晶体结构，揭示了其催化NAD+水解为ADPR和cADPR的分子机制，并阐明了二聚化对其酶活性的调控作用。
2. **文献名称**：*"Recombinant CD38 protein enhances daratumumab-mediated cytotoxicity in multiple myeloma models"*
**作者**：Overdijk, M.B., Jansen, J.H., Nederend, M., et al.
**摘要**：研究利用重组CD38蛋白验证了达雷妥尤单抗(Daratumumab)的结合表位，证明其通过抗体依赖性细胞毒性(ADCC)抑制多发性骨髓瘤细胞的生长，为临床疗效提供了分子基础。
3. **文献名称**：*"Functional characterization of CD38 variants expressed in HEK293 cells: Insights into enzyme kinetics and signaling roles"*
**作者**：Chini, E.N., Chini, C.C.S., Espindola Netto, J.M., et al.
**摘要**：通过在HEK293细胞中表达重组CD38蛋白，分析了其NAD+水解酶活性及在钙信号通路中的作用，发现CD38通过调控细胞内cADPR水平影响钙释放，进而调节免疫细胞功能。
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以上研究从结构解析、治疗靶点验证到功能机制探索，展现了CD38重组蛋白在基础与转化医学中的关键作用。
CD38. a type II transmembrane glycoprotein, is a multifunctional enzyme widely expressed on immune cells, including T cells, B cells, and natural killer cells, as well as non-immune tissues. Initially identified as a lymphocyte differentiation antigen, it gained prominence for its role in cell adhesion, signaling, and calcium homeostasis. CD38 functions as an ectoenzyme that catalyzes the hydrolysis of NAD+ (nicotinamide adenine dinucleotide) to produce cyclic ADP-ribose (cADPR) and ADP-ribose (ADPR), secondary messengers critical for intracellular calcium mobilization. This enzymatic activity links CD38 to metabolic regulation, aging, and immune responses.
In disease contexts, CD38 is overexpressed in hematological malignancies, such as multiple myeloma and chronic lymphocytic leukemia, making it a therapeutic target. Its surface expression on malignant cells has driven the development of anti-CD38 monoclonal antibodies (e.g., daratumumab) for immunotherapy. Beyond oncology, CD38 is implicated in autoimmune disorders and metabolic syndromes due to its regulatory effects on NAD+ metabolism and immune cell function.
Recombinant CD38 protein, produced via genetic engineering in systems like mammalian cells or bacteria, retains native enzymatic and structural properties. This allows researchers to study its biochemical mechanisms, screen inhibitors, or develop antibody-based therapies. Purified recombinant CD38 is essential for structural studies (e.g., X-ray crystallography), functional assays (e.g., NADase activity tests), and validating drug candidates in preclinical models. Its utility spans basic research, diagnostics, and biopharmaceutical development, underscoring its importance in both understanding disease pathways and advancing targeted therapies.
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