纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | CA9 |
Uniprot No | Q16790 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 59-414aa |
氨基酸序列 | PLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSL KLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAG RFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPP GLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTA FARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQV PGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHT LSDTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNS CLAAGD |
预测分子量 | 39 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CA9重组蛋白的3篇代表性文献及其摘要:
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1. **"Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix binding segment"**
*Authors: Pastorek J., et al. (1994)*
该研究首次克隆并鉴定了CA9(MN蛋白),发现其与碳酸酐酶家族同源,并在缺氧条件下高表达于多种癌细胞中,为后续重组蛋白功能研究奠定基础。
2. **"Hypoxia activates the capacity of tumor-associated carbonic anhydrase IX to acidify extracellular pH"**
*Authors: Svastova E., et al. (2003)*
通过重组CA9蛋白实验,揭示其在缺氧肿瘤微环境中通过调节细胞外pH促进肿瘤存活和侵袭的机制,强调了其作为治疗靶点的潜力。
3. **"Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX"**
*Authors: Lou Y., et al. (2011)*
利用X射线晶体学解析了CA9重组蛋白的催化结构域三维结构,揭示了其与抑制剂结合的分子机制,为靶向药物设计提供结构基础。
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*注:若需获取具体文献,建议通过PubMed或Sci-Hub输入标题/作者查询全文。*
Carbonic anhydrase IX (CA9), a zinc-containing metalloenzyme, has emerged as a critical biomarker and therapeutic target in cancer biology. Initially identified as a hypoxia-responsive gene product, CA9 is transcriptionally regulated by hypoxia-inducible factor (HIF)-1α under low-oxygen conditions. This transmembrane protein features a catalytic extracellular domain that regulates extracellular pH by converting CO₂ and water to bicarbonate and protons, a process crucial for maintaining cellular homeostasis in tumor microenvironments.
CA9 is overexpressed in numerous cancers, particularly clear cell renal cell carcinoma (ccRCC), where it correlates with poor prognosis, metastasis, and therapy resistance. Its restricted expression in normal tissues (primarily gastric mucosa) and widespread presence in hypoxic tumors make it an attractive target for precision therapies. Recombinant CA9 protein, typically produced in mammalian expression systems like HEK293 or CHO cells, retains the native structure and enzymatic activity required for functional studies. Advanced purification techniques, including affinity chromatography and tag-based systems, ensure high purity and batch-to-batch consistency.
In research, recombinant CA9 facilitates drug discovery by enabling high-throughput screening of inhibitors, such as monoclonal antibodies or small molecules targeting its extracellular domain. It also serves as a critical reagent in diagnostic assay development and antibody validation. Notably, CA9-targeted therapies, including antibody-drug conjugates and CAR-T cells, are under clinical evaluation, leveraging its tumor-specific expression to minimize off-target effects. Additionally, CA9’s role in chemoresistance via pH-mediated drug efflux underscores its therapeutic relevance. Ongoing studies explore its interplay with immune checkpoints and potential as a combined therapeutic modality. Validated by SDS-PAGE, Western blot, and enzymatic activity assays, recombinant CA9 remains indispensable for deciphering its pathophysiological mechanisms and advancing cancer therapeutics.
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