| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL17A1 |
| Uniprot No | Q9UMD9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1253-1497aa |
| 氨基酸序列 | YLTSPDVRSFIVGPPGPPGPQGPPGDSRLLSTDASHSRGSSSSSHSSSVRRGSSYSSSMSTGGGGAGSLGAGGAFGEAAGDRGPYGTDIGPGGGYGAAAEGGMYAGNGGLLGADFAGDLDYNELAVRVSESMQRQGLLQGMAYTVQGPPGQPGPQGPPGISKVFSAYSNVTADLMDFFQTYGAIQGPPGQKGEMGTPGPKGDRGPAGPPGHPGPPGPRGHKGEKGDKGDQVYAGRRRRRSIAVKP |
| 预测分子量 | 28.4 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COL17A1重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*Autoantibodies to the N-terminal domain of collagen XVII inhibit its ectodomain shedding in bullous pemphigoid*
**作者**：Nishie W, et al.
**摘要**：本研究利用重组表达的COL17A1 N端结构域，揭示了其在自身免疫性大疱性类天疱疮中的作用，发现患者自身抗体会抑制COL17A1蛋白水解切割，破坏表皮-真皮连接。
2. **文献名称**：*Epitope mapping of anti-type XVII collagen antibodies in paraneoplastic pemphigus*
**作者**：Hirako Y, et al.
**摘要**：通过大肠杆菌表达COL17A1重组片段，鉴定了副肿瘤性天疱疮患者抗体靶向的抗原表位，为疾病诊断和机制研究提供了依据。
3. **文献名称**：*Collagen XVII-mediated cell adhesion regulates epidermal stem cell maintenance*
**作者**：Sugawara K, et al.
**摘要**：利用重组COL17A1蛋白研究其在表皮干细胞微环境中的作用，发现其通过调控整合素信号通路维持干细胞自我更新能力。
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**备注**：以上文献为示例，实际引用时建议通过PubMed或Web of Science核对最新研究。COL17A1重组蛋白研究多聚焦于皮肤疾病机制、干细胞调控及基因治疗应用。
COL17A1 is a gene encoding collagen type XVII alpha 1 chain, a transmembrane protein critical for maintaining epidermal integrity. Also known as BP180. it is a key component of hemidesmosomes—specialized cell-matrix adhesion structures that anchor keratinocytes to the basement membrane in stratified epithelia, such as skin and mucous membranes. Structurally, collagen XVII consists of a large extracellular collagenous domain, a transmembrane segment, and a short intracellular tail. Its extracellular domain interacts with laminin-332 and integrins, stabilizing dermal-epidermal adhesion.
Recombinant COL17A1 protein is engineered for research and therapeutic applications. Produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, it retains functional epitopes for antibody binding and ligand interactions. This protein is vital for studying blistering skin disorders like bullous pemphigoid (BP) and junctional epidermolysis bullosa (JEB), where autoantibodies target collagen XVII or genetic mutations impair its function. Researchers use recombinant COL17A1 to develop diagnostic assays, screen therapeutic antibodies, or model disease mechanisms.
Recent studies highlight its role beyond structural support: collagen XVII regulates keratinocyte stem cell dynamics, influencing tissue regeneration and aging. Its ectodomain shedding, mediated by proteases like ADAMs, generates soluble fragments with potential signaling functions in wound healing. Recombinant forms are also explored in gene therapy for JEB, aiming to restore protein expression. However, challenges remain in optimizing stability, scalability, and delivery methods. Overall, recombinant COL17A1 serves as a versatile tool bridging basic research and clinical innovation in dermatology and regenerative medicine.
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