纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | COL12A1 |
Uniprot No | Q99715 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 140-316aa |
氨基酸序列 | DLVFLVDGSWSVGRNNFKYILDFIAALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYQRDELLAAIKKIPYKGGNTMTGDAIDYLVKNTFTESAGARVGFPKVAIIITDGKSQDEVEIPARELRNVGVEVFSLGIKAADAKELKQIASTPSLNHVFNVANFDAIVDIQNEIISQV |
预测分子量 | 23.5 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COL12A1重组蛋白的模拟参考文献示例(注:文献为虚构,仅供格式参考):
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1. **文献名称**: "Recombinant COL12A1 production and its role in extracellular matrix assembly"
**作者**: Smith A et al.
**摘要**: 本研究通过哺乳动物表达系统成功表达并纯化了重组COL12A1蛋白,证实其能够促进成纤维细胞的粘附和迁移,并参与III型胶原纤维的组装,为研究遗传性肌肉疾病提供了工具。
2. **文献名称**: "Functional characterization of COL12A1 variants using recombinant protein models"
**作者**: Zhang L et al.
**摘要**: 通过构建COL12A1重组突变体蛋白,分析了其在贝斯综合征中的致病机制,发现特定结构域突变会破坏胶原网络稳定性,导致皮肤脆性增加。
3. **文献名称**: "COL12A1 recombinant protein enhances tendon repair in vivo"
**作者**: Tanaka K et al.
**摘要**: 动物实验表明,局部递送重组COL12A1可显著加速肌腱损伤修复,其机制可能与激活整合素信号通路和抑制过度纤维化相关。
4. **文献名称**: "Structural insights into COL12A1-collagen VI interactions via recombinant domain mapping"
**作者**: Müller R et al.
**摘要**: 利用重组COL12A1片段进行结合实验,揭示了其与胶原VI的C端结构域特异性互作,为开发靶向细胞外基质的治疗策略提供依据。
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建议通过PubMed、Web of Science或Google Scholar搜索真实文献,关键词组合如:"COL12A1 recombinant protein"、"recombinant collagen XII production"或"COL12A1 in vitro expression"。
**Background of COL12A1 Recombinant Protein**
COL12A1 encodes the alpha-1 chain of type XII collagen, a member of the fibril-associated collagens with interrupted triple helices (FACIT) family. This extracellular matrix (ECM) protein plays a regulatory role in organizing fibrillar collagen networks, particularly type I collagen, influencing tissue integrity and biomechanical properties. Structurally, type XII collagen consists of a large N-terminal non-collagenous domain and a collagenous domain with multiple interruptions, enabling flexible interactions with other ECM components.
Recombinant COL12A1 protein is engineered to study its functional roles in vitro and in vivo. Produced via mammalian expression systems (e.g., HEK293 cells), it retains post-translational modifications critical for stability and binding activity, such as hydroxylation and glycosylation. Purification methods often involve affinity tags (e.g., His-tag) followed by chromatography.
Research highlights its involvement in cell adhesion, migration, and mechanotransduction by interacting with integrins and other receptors. It also modulates tissue remodeling in development, wound healing, and pathologies like fibrosis. Mutations in COL12A1 are linked to musculoskeletal disorders, including a subtype of Ehlers-Danlos syndrome (EDS), characterized by hypermobility and fragile connective tissues. Recombinant COL12A1 serves as a tool to explore disease mechanisms, screen therapeutics, or engineer biomimetic scaffolds for regenerative medicine.
Current studies focus on its dual role as both a structural and signaling molecule, bridging ECM dynamics with cellular responses. Its tissue-specific isoforms and context-dependent functions remain areas of active investigation, underscoring its potential as a target for ECM-related therapies.
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