| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | COL4 |
| Uniprot No | Q940T9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-362aa |
| 氨基酸序列 | MASKLCDSCKSATAALYCRPDAAFLCLSCDSKVHAANKLASRHARVWMCEVCEQAPAHVTCKADAAALCVTCDRDIHSANPLARRHERVPVTPFYDSVSSDGSVKHTAVNFLDDCYFSDIDGNGSREEEEEEAASWLLLPNPKTTTTATAGIVAVTSAEEVPGDSPEMNTGQQYLFSDPDPYLDLDYGNVDPKVESLEQNSSGTDGVVPVENRTVRIPTVNENCFEMDFTGGSKGFTYGGGYNCISHSVSSSSMEVGVVPDGGSVADVSYPYGGPATSGADPGTQRAVPLTSAEREARVMRYREKRKNRKFEKTIRYASRKAYAEMRPRIKGRFAKRTDTNESNDVVGHGGIFSGFGLVPTF |
| 预测分子量 | 39,1 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3条关于COL4重组蛋白的经典文献及其摘要概括：
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1. **文献名称**: *"Recombinant collagen IV α1-chain non-collagenous domain efficiently inhibits angiogenesis and tumor growth"*
**作者**: Sudhakar, A. et al.
**摘要**: 该研究利用重组表达技术制备了IV型胶原蛋白α1链的非胶原结构域(NC1)，证明其能通过抑制内皮细胞迁移和血管生成，显著减缓小鼠模型中的肿瘤生长。
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2. **文献名称**: *"Structural and functional analysis of the recombinant α3α4α5 heterotrimer of human collagen IV"*
**作者**: Khoshnoodi, J. et al.
**摘要**: 作者通过哺乳动物细胞重组系统成功表达并纯化了人源IV型胶原蛋白的α3α4α5异源三聚体，解析了其三维结构，并发现其与遗传性肾病(如Alport综合征)相关的突变会破坏基底膜的稳定性。
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3. **文献名称**: *"Recombinant collagen-like proteins as biomimetic materials for tissue engineering"*
**作者**: Peng, Y.Y. et al.
**摘要**: 研究设计了一种重组类IV型胶原蛋白仿生材料，验证其在体外支持细胞黏附和增殖的能力，为组织工程中基底膜仿生支架的开发提供了新策略。
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如需具体文献年份或数据库链接，可进一步通过PubMed或Sci-Hub检索标题或作者获取原文。
Collagen type IV (COL4) is a critical structural component of basement membranes, specialized extracellular matrices that provide structural support and regulate cellular behavior in various tissues. Composed of six distinct α chains (α1–α6), COL4 forms a flexible, sheet-like network through the assembly of triple-helical protomers. These protomers typically consist of α1α1α2 heterotrimers in most basement membranes, while α3α4α5 heterotrimers are tissue-specific, notably in the kidney glomeruli, cochlea, and eye. COL4's unique structure, featuring interrupted Gly-X-Y repeats and non-collagenous domains, enables both mechanical stability and molecular signaling functions.
Recombinant COL4 proteins are engineered using expression systems (e.g., mammalian, insect, or yeast cells) to reproduce specific chain combinations. This technology addresses challenges in isolating native COL4. which is prone to proteolytic degradation and exists in complex tissue matrices. Recombinant forms preserve critical biological activities, including cell adhesion via integrin-binding motifs (e.g., GFOGER sequences) and interactions with laminins/nidogens.
Research applications focus on modeling basement membrane-related pathologies, such as Alport syndrome (caused by COL4A3/A4/A5 mutations), diabetic nephropathy, and tumor angiogenesis. In regenerative medicine, recombinant COL4 scaffolds enhance in vitro 3D tissue models and promote endothelial/epithelial cell differentiation. Recent advances include chimeric COL4 variants with modified bioavailability and hybrid matrices combining multiple basement membrane components. However, production complexities persist due to COL4's large size (~1.800 residues per chain) and post-translational modifications. Current efforts optimize folding efficiency and chain pairing to better mimic native supramolecular architectures for therapeutic and diagnostic applications.
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