| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL12 |
| Uniprot No | Q9LJ44 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-364aa |
| 氨基酸序列 | MEPKCDHCAT SQALIYCKSD LAKLCLNCDV HVHSANPLSH RHIRSLICEK CFSQPAAIRC LDEKVSYCQG CHWHESNCSE LGHRVQSLNP FSGCPSPTDF NRMWSSILEP PVSGLLSPFV GSFPLNDLNN TMFDTAYSMV PHNISYTQNF SDNLSFFSTE SKGYPDMVLK LEEGEEDLCE GLNLDDAPLN FDVGDDIIGC SSEVHIEPDH TVPNCLLIDK TNTSSFTGSN FTVDKALEAS PPGQQMNINT GLQLPLSPVL FGQIHPSLNI TGENNAADYQ DCGMSPGFIM SEAPWETNFE VSCPQARNEA KLRYKEKKLK RSFGKQIRYA SRKARADTRK RVKGRFVKAG DSYDYDPSSP TTNN |
| 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COL12重组蛋白的3篇文献摘要信息：
1. **文献名称**：*"Recombinant collagen XII produced in mammalian cells reveals tissue-specific structures and functions"*
**作者**：Smith A, et al.
**摘要**：研究利用哺乳动物细胞系统表达重组COL12蛋白，证实其形成三聚体结构，并揭示其在调控细胞外基质柔韧性及细胞黏附中的功能，尤其在肌腱组织中的力学信号传递作用。
2. **文献名称**：*"Engineering and characterization of a collagen XII heterotrimer for in vitro matrix assembly studies"*
**作者**：Chen L, et al.
**摘要**：通过基因工程构建重组COL12异源三聚体，证明其可与胶原I/III纤维共组装，并调节基质刚度，为研究COL12在纤维化疾病中的分子机制提供工具。
3. **文献名称**：*"Collagen XII interacts with avian integrin receptors to mediate cellular responses"*
**作者**：Böhm H, et al.
**摘要**：利用昆虫细胞表达系统获得重组COL12的NC3结构域，发现其通过结合整合素α2β1激活FAK信号通路，促进成纤维细胞迁移，提示其在伤口修复中的潜在应用价值。
注：以上文献信息为示例性质，实际研究中请根据具体需求检索PubMed或Web of Science获取原文。
Collagen type XII (COL12) is a member of the fibril-associated collagens with interrupted triple helices (FACIT) family, primarily found in tissues rich in type I and III collagens, such as tendons, skin, and connective tissues. It plays a regulatory role in organizing the extracellular matrix (ECM) by interacting with other collagen fibrils and non-collagenous components. Structurally, COL12 consists of three identical α1(XII) chains forming a homotrimeric triple helix, flanked by large non-collagenous domains (NC3) at its N-terminus. These domains facilitate interactions with ECM proteins, proteoglycans, and cell-surface receptors, influencing tissue mechanics and cell signaling.
COL12 is critical during embryonic development, wound healing, and tissue remodeling, where it modulates collagen fibrillogenesis and ECM stability. Its expression is dynamically regulated in response to mechanical stress, inflammation, or injury. Dysregulation of COL12 has been linked to musculoskeletal disorders, including congenital myopathies, Ehlers-Danlos syndrome-like phenotypes, and fibrosis. Mutations in the COL12A1 gene are associated with Bethlem myopathy and Ullrich congenital muscular dystrophy, highlighting its role in maintaining tissue integrity.
Recombinant COL12 proteins are engineered to study its structural-functional relationships, ECM assembly mechanisms, and therapeutic potential. Produced via mammalian or insect cell systems, these proteins retain post-translational modifications (e.g., hydroxylation, glycosylation) essential for biological activity. Applications include in vitro ECM modeling, drug screening for fibrosis or connective tissue diseases, and biomaterial development for regenerative medicine. Research on COL12 also explores its crosstalk with integrins and growth factors, offering insights into tissue-specific matrix adaptations and disease pathways.
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