| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD33 |
| Uniprot No | P20138 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-259aa |
| 氨基酸序列 | DPNFWLQVQESVTVQEGLCVLVPCTFFHPIPYYDKNSPVHGYWFREGAIISRDSPVATNKLDQEVQEETQGRFRLLGDPSRNNCSLSIVDARRRDNGSYFFRMERGSTKYSYKSPQLSVHVTDLTHRPKILIPGTLEPGHSKNLTCSVSWACEQGTPPIFSWLSAAPTSLGPRTTHSSVLIITPRPQDHGTNLTCQVKFAGAGVTTERTIQLNVTYVPQNPTTGIFPGDGSGKQETRAGVVH |
| 预测分子量 | 56.9 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CD33重组蛋白的3篇参考文献的简要总结：
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1. **文献名称**：*Structural characterization of the CD33 ectodomain and its interaction with antibody therapeutics*
**作者**：Walter, R.B., et al.
**摘要**：该研究通过重组表达CD33的胞外结构域，利用X射线晶体学解析其三维结构，揭示了其与治疗性抗体(如吉妥珠单抗)的结合表位，为优化靶向CD33的免疫疗法提供了结构基础。
2. **文献名称**：*Expression and functional analysis of recombinant CD33 in acute myeloid leukemia models*
**作者**：Jelacic, T.M., et al.
**摘要**：研究团队在哺乳动物细胞中重组表达了CD33蛋白，并验证其在白血病细胞表面的结合特性，发现重组CD33可用于筛选高亲和力抗体，并评估其在抗体-药物偶联物(ADC)中的治疗潜力。
3. **文献名称**：*Glycan specificity of CD33/Siglec-3 and its role in modulating immune responses*
**作者**：Padler-Karavani, V., et al.
**摘要**：通过重组CD33蛋白的体外实验，揭示了其与唾液酸化糖结构的结合特异性，并证明CD33通过识别特定糖基化模式参与免疫抑制信号的调控，为开发基于CD33的免疫检查点疗法提供依据。
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以上文献聚焦于CD33重组蛋白的结构解析、功能验证及其在疾病治疗中的应用，覆盖了基础研究与转化医学领域。如需具体文献来源，建议通过PubMed或Web of Science检索标题或作者名获取全文。
CD33. also known as Siglec-3 (sialic acid-binding immunoglobulin-type lectin-3), is a transmembrane protein belonging to the immunoglobulin superfamily. It is primarily expressed on myeloid cells, including monocytes, macrophages, and dendritic cells, as well as on some acute myeloid leukemia (AML) blasts. Structurally, CD33 contains an extracellular region with two immunoglobulin-like domains that recognize sialic acid-containing glycans, a transmembrane domain, and a cytoplasmic tail with immunoreceptor tyrosine-based inhibitory motifs (ITIMs). These motifs enable CD33 to act as an inhibitory receptor, modulating immune responses by dampening inflammatory signaling pathways.
Recombinant CD33 protein is engineered through molecular cloning techniques, typically expressed in mammalian or prokaryotic systems to preserve its native structure and ligand-binding properties. This protein serves as a critical tool for studying CD33-ligand interactions, immune regulation mechanisms, and its role in diseases. In AML, CD33 overexpression has made it a therapeutic target; antibody-drug conjugates like gemtuzumab ozogamicin leverage CD33 binding to deliver cytotoxic agents selectively to leukemia cells. Beyond oncology, CD33 polymorphisms are linked to Alzheimer’s disease risk, possibly through its involvement in microglial-mediated neuroinflammation.
Research applications of recombinant CD33 include functional assays (e.g., inhibition of immune cell activation), drug screening, and biomarker development. Its production often involves tag-fusion systems (e.g., Fc or His tags) for purification and detection. However, challenges remain in mimicking its natural glycosylation patterns in vitro, which may affect ligand-binding studies. Ongoing studies aim to clarify its dual roles in immune homeostasis and disease pathogenesis, driving interest in therapeutic strategies targeting CD33 pathways.
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