| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBD |
| Uniprot No | P02042 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-147aa |
| 氨基酸序列 | VHLTPEEKTAVNALWGKVNVDAVGGEALGRLLVVYPWTQRFFESFGDLSSPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFSQLSELHCDKLHVDPENFRLLGNVLVCVLARNFGKEFTPQMQAAYQKVVAGVANALAHKYH |
| 预测分子量 | 47.5 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3篇关于HBD(肝素结合结构域)重组蛋白的参考文献示例(注：部分内容为示例性概括，实际文献需根据具体研究检索)：
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1. **文献名称**：*Recombinant HBD-fibronectin fusion protein enhances cell adhesion in biomaterials*
**作者**：Zhang Y, et al.
**摘要**：研究构建了HBD与纤连蛋白的重组融合蛋白，证明其能通过肝素结合特性显著提升细胞在生物材料表面的粘附效率，为组织工程支架涂层提供了新策略。
2. **文献名称**：*HBD-mediated growth factor delivery accelerates wound healing in diabetic mice*
**作者**：Lee S, Kim JH.
**摘要**：开发了基于HBD的重组蛋白载体系统，用于缓释血管内皮生长因子(VEGF)。动物实验显示，该系统可提高药物滞留时间并促进糖尿病模型小鼠的创面愈合。
3. **文献名称**：*Expression and purification of recombinant HBD-linked antimicrobial peptides in E. coli*
**作者**：Wang X, et al.
**摘要**：报道了一种在大肠杆菌中高效表达HBD-抗菌肽重组蛋白的方法，通过肝素亲和层析纯化获得高活性产物，验证其对多重耐药菌的抑制作用。
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如需具体文献，建议通过PubMed或Google Scholar检索关键词“heparin-binding domain recombinant protein”+应用领域(如drug delivery/tissue engineering)。
Human beta-defensins (HBDs) are a family of small cationic antimicrobial peptides (AMPs) that play critical roles in innate immunity. First identified in the 1990s, HBDs are primarily secreted by epithelial cells at mucosal surfaces and skin, functioning as the body’s first line of defense against pathogens. These evolutionarily conserved peptides exhibit broad-spectrum antimicrobial activity against bacteria, viruses, and fungi while modulating immune responses through chemotaxis and activation of immune cells. The human genome encodes multiple HBD isoforms (e.g., HBD-1. HBD-2. HBD-3), each with distinct expression patterns and antimicrobial profiles.
Recombinant HBD production emerged as a solution to overcome the limitations of natural extraction, which yields minimal quantities. Using genetic engineering techniques, synthetic genes encoding specific HBD isoforms are inserted into expression vectors (commonly E. coli, yeast, or mammalian cells) for large-scale production. This approach allows precise control over peptide sequences and post-translational modifications. Recombinant HBDs retain the native structure and function, enabling standardized research and therapeutic applications.
Interest in HBD-based therapeutics has grown due to antibiotic resistance concerns. Preclinical studies highlight their potential in treating infections, chronic wounds, and inflammatory diseases. However, challenges persist, including peptide stability in vivo, potential cytotoxicity at high concentrations, and delivery optimization. Current research focuses on engineering hybrid peptides, nano-carrier systems, and topical formulations to enhance clinical efficacy. As natural immune modulators with low resistance development risk, recombinant HBDs represent a promising frontier in antimicrobial and immunotherapeutic development.
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