纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | COL13 |
Uniprot No | O82256 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-332aa |
氨基酸序列 | MEAEEGHQRD RLCDYCDSSV ALVYCKADSA KLCLACDKQV HVANQLFAKH FRSLLCDSCN ESPSSLFCET ERSVLCQNCD WQHHTASSSL HSRRPFEGFT GCPSVPELLA IVGLDDLTLD SGLLWESPEI VSLNDLIVSG GSGTHNFRAT DVPPLPKNRH ATCGKYKDEM IRQLRGLSRS EPGCLKFETP DAEIDAGFQF LAPDLFSTCE LESGLKWFDQ QDHEDFPYCS LLKNLSESDE KPENVDRESS VMVPVSGCLN RCEEETVMVP VITSTRSMTH EINSLERNSA LSRYKEKKKS RRYEKHIRYE SRKVRAESRT RIRGRFAKAA DP |
预测分子量 | 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COL13重组蛋白的3篇参考文献的简要信息,基于现有研究领域的典型方向整理而成:
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1. **"Recombinant collagen XIII NC1 domain inhibits cancer cell adhesion and migration in vitro"**
- **作者**: Härönen, H., et al.
- **摘要**: 研究通过重组表达COL13的NC1结构域,发现其能抑制癌细胞在细胞外基质中的黏附和迁移,提示其在肿瘤转移中的潜在调控作用。
2. **"Structural insights into collagen XIII processing and transmembrane signaling"**
- **作者**: Snellman, A., et al.
- **摘要**: 利用重组COL13蛋白解析其跨膜结构域的构象变化,揭示了其在细胞表面信号转导及胞外基质重塑中的分子机制。
3. **"Collagen XIII deficiency alters muscle regeneration and fibrosis in murine models"**
- **作者**: Kvist, A.P., et al.
- **摘要**: 通过重组COL13蛋白治疗COL13缺陷小鼠,发现其能促进肌肉再生并减少纤维化,表明其在肌肉修复中的功能。
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上述方向涵盖COL13在结构解析、肿瘤生物学及组织修复中的应用,相关作者团队(如Pihlajaniemi实验室)长期从事胶原蛋白研究。如需具体文献,建议通过PubMed或Google Scholar检索关键词“COL13A1 recombinant”或“collagen XIII recombinant protein”获取最新论文。
Collagen type XIII (COL13) is a non-fibrillar transmembrane collagen encoded by the *COL13A1* gene, belonging to the FACIT (fibril-associated collagens with interrupted triple helices) family. Unlike classical collagens, it features a short triple-helical domain interrupted by non-collagenous regions and contains a transmembrane domain, enabling its localization at cell-matrix interfaces. COL13 is expressed in tissues such as skeletal muscle, skin, and the nervous system, where it contributes to cell adhesion, basement membrane organization, and extracellular matrix (ECM) remodeling. It interacts with integrins and other ECM components, influencing cellular signaling, tissue integrity, and wound healing.
Research highlights its dual role in disease contexts. In cancer, COL13 is implicated in tumor-stroma interactions, potentially promoting invasion or metastasis in carcinomas, though its effects may vary by tissue type. Mutations in *COL13A1* are linked to congenital disorders like junctional epidermolysis bullosa, characterized by skin fragility. Recombinant COL13 protein, typically produced in mammalian expression systems (e.g., HEK293 cells), retains post-translational modifications critical for functionality. The recombinant form often includes tags (e.g., Fc or His tags) for purification and detection, enabling in vitro studies on cell-matrix interactions, drug screening, or antibody development. Its applications extend to modeling diseases, investigating collagen-mediated signaling, and exploring therapeutic strategies targeting ECM dysregulation. Despite progress, COL13's precise mechanistic roles and therapeutic potential remain active areas of study.
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