| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL5a2 |
| Uniprot No | P05997 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1499aa |
| 氨基酸序列 | MMANWAEARPLLILIVLLGQFVSIKAQEEDEDEGYGEEIACTQNGQMYLNRDIWKPAPCQICVCDNGAILCDKIECQDVLDCADPVTPPGECCPVCSQTPGGGNTNFGRGRKGQKGEPGLVPVVTGIRGRPGPAGPPGSQGPRGERGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGLSRPFSAQMAGLDEKSGLGSQVGLMPGSVGPVGPRGPQGLQGQQGGAGPTGPPGEPGDPGPMGPIGSRGPEGPPGKPGEDGEPGRNGNPGEVGFAGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEVGAPGSKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGQRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPVGSPGLPGAIGTDGTPGAKGPTGSPGTSGPPGSAGPPGSPGPQGSTGPQGIRGQPGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPVGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGSQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDPGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKPGDQGVPGDPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGSPGPSGTPGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPNGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPLGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGGPGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGDPGSRGPIGPPGRAGKRGLPGPQGPRGDKGDHGDRGDRGQKGHRGFTGLQGLPGPPGPNGEQGSAGIPGPFGPRGPPGPVGPSGKEGNPGPLGPIGPPGVRGSVGEAGPEGPPGEPGPPGPPGPPGHLTAALGDIMGHYDESMPDPLPEFTEDQAAPDDKNKTDPGVHATLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHSAKQSGEYWIDPNQGSVEDAIKVYCNMETGETCISANPSSVPRKTWWASKSPDNKPVWYGLDMNRGSQFAYGDHQSPNTAITQMTFLRLLSKEASQNITYICKNSVGYMDDQAKNLKKAVVLKGANDLDIKAEGNIRFRYIVLQDTCSKRNGNVGKTVFEYRTQNVARLPIIDLAPVDVGGTDQEFGVEIGPVCFV |
| 预测分子量 | 144,9 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. |
以下为模拟生成的参考文献示例(非真实文献，仅供格式参考)：
1. **标题**：Recombinant human COL5A2 production in mammalian cells and its role in collagen fibrillogenesis
**作者**：Smith A, et al.
**摘要**：研究利用HEK293细胞表达重组COL5A2蛋白，证实其与COL5A1共同形成V型胶原异源三聚体，并通过体外实验证明其调控胶原纤维直径的作用。
2. **标题**：Functional analysis of COL5A2 mutations in Ehlers-Danlos syndrome using recombinant protein models
**作者**：Chen L, et al.
**摘要**：通过重组COL5A2蛋白构建点突变体，发现特定结构域突变导致胶原分泌障碍，为经典EDS发病机制提供分子证据。
3. **标题**：Expression and purification of recombinant COL5A2 for extracellular matrix biomaterial development
**作者**：Yamamoto K, et al.
**摘要**：报道在大肠杆菌中可溶性表达COL5A2片段的方法，并验证其在促进成纤维细胞粘附和增殖中的生物活性。
4. **标题**：Structural insights into COL5A2 C-propeptide interactions via recombinant domain mapping
**作者**：Birk DE, et al.
**摘要**：利用重组COL5A2 C端前肽蛋白，结合SPR技术解析其与整合素受体的结合位点，揭示其在胶原组装中的调控机制。
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**注意**：以上内容为模拟示例，实际文献需通过PubMed/Google Scholar等平台检索(关键词：COL5A2 recombinant, type V collagen expression)。真实研究可能集中在COL5A2的疾病关联或复合胶原表达体系。
**Background of COL5A2 Recombinant Protein**
COL5A2 (Collagen Type V Alpha 2 Chain) is a critical component of type V collagen, a fibrillar collagen found predominantly in connective tissues. Type V collagen is essential for regulating the assembly and diameter of heterotypic collagen fibrils, particularly those formed with type I collagen, which contribute to the structural integrity of skin, tendons, bones, and other extracellular matrices. The COL5A2 gene encodes the α2 chain of type V collagen, which combines with α1 chains (COL5A1 or COL5A3) to form triple-helical procollagen molecules. These are enzymatically processed into mature collagen fibrils, playing a role in tissue organization and mechanical stability.
Recombinant COL5A2 protein is produced via genetic engineering, often using mammalian or insect cell systems to ensure proper post-translational modifications, such as hydroxylation and glycosylation, critical for collagen functionality. This engineered protein retains the structural and bioactive properties of native COL5A2. enabling researchers to study its interactions in vitro or in vivo.
Mutations in COL5A2 are linked to Ehlers-Danlos syndrome (EDS), a group of disorders characterized by skin hyperelasticity, joint hypermobility, and tissue fragility. Recombinant COL5A2 serves as a tool to investigate disease mechanisms, screen therapeutic agents, or engineer biomimetic scaffolds for regenerative medicine. Its applications extend to studying cell-matrix interactions, fibrosis, and wound healing, offering insights into tissue repair strategies. By mimicking natural collagen behavior, recombinant COL5A2 also aids in developing biocompatible materials for clinical use.
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