Recombinant Human CDA protein

中文名： 胞苷脱氨酶(CDA)重组蛋白
别名： CDA；HR1；JPO2；R1；Cell division cycle-associated 7-like protein

货号: PA1000-8027

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	CDA
Uniprot No	P32320
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-146aa
氨基酸序列	MGSSHHHHHHSSGLVPRGSHMAQKRPACTLKPECVQQLLVCSQEAKQSAY CPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYK DFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQ ELLPSSFGPEDLQKTQ
预测分子量	18 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.

参考文献

以下是关于CDA(胞苷脱氨酶)重组蛋白的参考文献示例，包括文献名称、作者及摘要内容概括：

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1. **《High-Yield Expression and Purification of Recombinant Human CDA in E. coli》**

**作者：Zhang et al. (2020)**

**摘要**：研究报道了通过大肠杆菌表达系统高效生产重组人CDA蛋白的优化策略，采用亲和层析纯化并验证其酶活性，为大规模制备用于生化研究的CDA提供方法。

2. **《Structural Insights into CDA’s Catalytic Mechanism via X-ray Crystallography》**

**作者：Lee et al. (2018)**

**摘要**：通过X射线晶体学解析了CDA重组蛋白的三维结构，揭示了其底物结合位点及催化残基，阐明了胞苷脱氨反应的分子机制。

3. **《CDA Recombinant Protein Enhances Chemotherapy Sensitivity in Pancreatic Cancer Models》**

**作者：Wang et al. (2021)**

**摘要**：体外实验表明，重组CDA蛋白可代谢吉西他滨前药，降低癌细胞耐药性，提示其作为化疗增敏剂的潜在应用价值。

4. **《Functional Characterization of a Novel CDA Variant in Antiviral Therapy》**

**作者：Smith et al. (2019)**

**摘要**：研究克隆并表征了一种新型CDA重组变体，证明其能有效降解病毒RNA中的修饰核苷，为开发广谱抗病毒药物提供理论依据。

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**注**：上述文献信息为示例性内容，实际引用时需以真实发表的论文为准，并核对作者、年份及期刊名称的准确性。

背景信息

CDA (Cytidine Deaminase) recombinant protein is a biotechnologically engineered enzyme derived from natural cytidine deaminases, which catalyze the hydrolytic deamination of cytidine to uridine or deoxycytidine to deoxyuridine. This class of enzymes plays critical roles in nucleotide metabolism, DNA repair, and epigenetic regulation. The recombinant form is typically produced using expression systems such as *E. coli*, yeast, or mammalian cells, enabling large-scale purification for research and therapeutic applications.

Interest in CDA recombinant protein surged with its implications in cancer therapy. For instance, it is involved in the activation or detoxification of nucleoside analogs like gemcitabine and 5-azacytidine, widely used chemotherapeutic agents. Variations in endogenous CDA activity among individuals can influence drug efficacy and toxicity, driving demand for standardized recombinant versions to study metabolic pathways or develop companion diagnostics.

Additionally, CDA has garnered attention in gene editing and antiviral research. Its ability to mediate targeted base conversions (e.g., cytosine to uracil) aligns with emerging CRISPR/Cas9-based base-editing technologies. In virology, CDA homologs are explored for their potential to introduce mutations in viral genomes, inhibiting replication.

The development of CDA recombinant proteins also addresses challenges in enzyme stability and substrate specificity. Engineering efforts, including site-directed mutagenesis and fusion tags, enhance catalytic efficiency and solubility for *in vitro* applications. Commercial variants often feature optimized codons, His-tags for purification, or thermostable mutations.

Overall, CDA recombinant protein serves as a versatile tool in molecular biology, oncology, and genetic engineering, bridging fundamental research with translational innovations in personalized medicine and biomanufacturing.