| 纯度 | >90%SDS-PAGE. |
| 种属 | Clostridium |
| 靶点 | colA |
| Uniprot No | P43153 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 90-370aa |
| 氨基酸序列 | NKIYTFDELNRMNYSDLVELIKTISYENVPDLFNFNDGSYTFFSNRDRVQAIIYGLEDSGRTYTADDDKGIPTLVEFLRAGYYLGFYNKQLSYLNTPQLKNECLPAMKAIQYNSNFRLGTKAQDGVVEALGRLIGNASADPEVINNCIYVLSDFKDNIDKYGSNYSKGNAVFNLMKGIDYYTNSVIYNTKGYDAKNTEFYNRIDPYMERLESLCTIGDKLNNDNAWLVNNALYYTGRMGKFREDPSISQRALERAMKEYPYLSYQYIEAANDLDLNFGGKN |
| 预测分子量 | 39.7 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“colA重组蛋白”的示例参考文献(注：文献为虚构示例，仅供格式参考)：
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1. **文献名称**：*High-Yield Expression and Purification of Recombinant colA Protein in E. coli*
**作者**：Zhang et al. (2020)
**摘要**：研究通过优化大肠杆菌表达系统，成功实现colA基因的高效表达，并开发了基于亲和层析的纯化方法，为后续功能研究提供基础。
2. **文献名称**：*Functional Characterization of colA-Encoded Collagenase in Bacterial Pathogenesis*
**作者**：Smith & Lee (2018)
**摘要**：探讨colA基因编码的胶原酶在病原菌侵袭宿主过程中的作用，通过重组蛋白实验验证其降解胶原蛋白的能力及对感染的影响。
3. **文献名称**：*Application of Recombinant colA Collagen in Tissue Engineering Scaffolds*
**作者**：Wang et al. (2021)
**摘要**：利用重组colA胶原蛋白构建3D生物支架，证明其具有良好的生物相容性和促进细胞黏附的特性，适用于组织修复。
4. **文献名称**：*Optimizing Fermentation Conditions for colA Production in Pichia pastoris*
**作者**：Chen et al. (2019)
**摘要**：在毕赤酵母中表达重组colA蛋白，通过调控培养温度、pH及诱导剂浓度显著提高产量，为工业化生产提供参考。
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如需真实文献，建议通过PubMed或Google Scholar搜索关键词(如“recombinant colA protein”、“colA gene expression”)获取。
ColA recombinant protein, commonly derived from the collagenase gene (colA) of *Clostridium histolyticum*, is a biotechnologically engineered enzyme widely studied for its collagenolytic activity. Collagenases are metalloproteases that specifically hydrolyze collagen, a major structural protein in connective tissues, making them valuable in both therapeutic and research applications. The colA gene encodes a multi-domain enzyme consisting of a catalytic domain responsible for collagen degradation and ancillary domains that enhance substrate binding and specificity. Recombinant production of ColA involves cloning the gene into expression vectors (e.g., *E. coli* or yeast systems), followed by purification using chromatographic techniques to ensure high purity and activity.
In biomedical contexts, ColA recombinant protein is utilized for tissue dissociation, wound debridement, and treating fibrotic disorders by breaking down excess collagen deposits. Its controlled enzymatic activity offers advantages over native collagenases, which often exhibit batch variability. In research, it facilitates cell isolation from tissues, 3D cell culture models, and extracellular matrix (ECM) studies. Additionally, engineered variants of ColA with modified substrate specificity or stability are being explored to optimize therapeutic efficacy and minimize off-target effects. Despite its utility, challenges such as immunogenicity and precise activity regulation in vivo require ongoing investigation. Overall, ColA recombinant protein represents a critical tool in regenerative medicine, drug development, and molecular biology, bridging microbial enzymology with advanced clinical applications.
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