首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBEGF |
| Uniprot No | Q99075 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 63-148aa |
| 氨基酸序列 | DLQEADLDLLRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKY KDFCIHGECKYVKELRAPSCICHPGYHGERCHGLSL |
| 预测分子量 | 10 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HBEGF重组蛋白的研究文献摘要概述(文献信息为模拟示例)：
1. **"Recombinant HBEGF promotes cell proliferation and wound healing in vitro"**
- 作者：Smith A et al.
- 摘要：研究通过大肠杆菌表达系统制备重组HBEGF蛋白，证实其能显著增强上皮细胞和成纤维细胞的增殖能力，并加速体外伤口愈合模型中的修复过程。
2. **"HBEGF recombinant protein mitigates chemotherapy-induced intestinal mucositis"**
- 作者：Chen L et al.
- 摘要：在小鼠模型中，注射重组HBEGF蛋白减少了化疗药物导致的肠道黏膜损伤，机制与激活EGFR/ERK信号通路及抑制细胞凋亡有关。
3. **"Structural and functional analysis of heparin-binding domain in HBEGF"**
- 作者：Yamamoto K et al.
- 摘要：通过基因工程截断突变实验，发现HBEGF的肝素结合结构域对其在细胞外基质的定位及促血管生成功能至关重要，重组蛋白缺失该区域后活性显著降低。
(注：以上为示例性内容，实际文献需通过PubMed或Google Scholar检索获取。)
**Background of HBEGF Recombinant Protein**
HBEGF (Heparin-Binding EGF-like Growth Factor) is a member of the epidermal growth factor (EGF) family, initially identified as a secreted protein with mitogenic activity for fibroblasts and smooth muscle cells. It is synthesized as a transmembrane precursor protein (proHBEGF) that undergoes proteolytic cleavage to release a soluble, biologically active form. The mature HBEGF consists of an EGF-like domain responsible for binding to EGF receptors (EGFR/ErbB1 and ErbB4) and a heparin-binding domain that facilitates interactions with cell-surface heparan sulfate proteoglycans, enhancing its local concentration and signaling efficacy.
HBEGF plays critical roles in diverse physiological and pathological processes, including cell proliferation, migration, survival, and tissue repair. It is implicated in wound healing, angiogenesis, and embryogenesis, but its dysregulation is also linked to cancer progression, atherosclerosis, and inflammatory diseases. In cancer, HBEGF overexpression promotes tumor growth, metastasis, and resistance to therapy by activating EGFR-mediated pathways.
Recombinant HBEGF protein is engineered using expression systems (e.g., mammalian, bacterial) to produce purified, bioactive forms for research and therapeutic applications. Its recombinant version enables precise study of EGFR signaling mechanisms and exploration of therapeutic strategies, such as targeting HBEGF-EGFR axis in cancers or leveraging its regenerative properties in tissue engineering.
Current research focuses on HBEGF's dual role in health and disease, aiming to develop inhibitors (e.g., monoclonal antibodies) for cancer therapy or harness its trophic effects for regenerative medicine. Its heparin-binding property is also exploited for drug delivery systems, enhancing targeting efficiency. Overall, HBEGF recombinant protein remains a vital tool for understanding EGFR biology and translating insights into clinical interventions.
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