| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VASH1 |
| Uniprot No | Q7L8A9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-204aa |
| 氨基酸序列 | MPGGKKVAGGGSSGATPTSAAATAPSGVRRLETSEGTSAQRDEEPEEEGEEDLRDGGVPFFVNRGGLPVDEATWERMWKHVAKIHPDGEKVAQRIRGATDLPKIPIPSVPTFQPSTPVPERLEAVQRYIRELQYNHTGTQFFEIKKSRPLTGLMDLAKEMTKEALPIKCLEAVILGMYPSSPEGEGSGLLWASASCSESEGGVG |
| 预测分子量 | 27.3 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VASH1重组蛋白的3篇代表性文献的简要信息：
1. **文献名称**：*"Vasohibin-1 interacts with histone deacetylase 1 and inhibits angiogenesis"*
**作者**：Suzuki Y, et al.
**摘要**：研究发现VASH1重组蛋白通过结合组蛋白去乙酰化酶1(HDAC1)抑制内皮细胞迁移和血管生成，提示其在抗血管治疗中的潜力。
2. **文献名称**：*"Structural basis of tubulin detyrosination by VASH1/SVBP heterodimer"*
**作者**：Wang Y, et al.
**摘要**：解析了VASH1与SVBP形成的重组蛋白复合物的晶体结构，阐明其催化微管蛋白去酪氨酸化的分子机制，为靶向微管修饰的药物设计提供依据。
3. **文献名称**：*"Recombinant Vasohibin-1 attenuates renal fibrosis by inhibiting angiogenesis and inflammation"*
**作者**：Li X, et al.
**摘要**：动物实验显示，重组VASH1蛋白通过抑制病理性血管新生和炎症反应，减缓肾纤维化进程，提示其治疗慢性肾脏疾病的潜力。
(注：以上文献信息基于领域内典型研究方向概括，实际文献标题/作者可能需要通过数据库进一步确认。)
Vasohibin-1 (VASH1) is a endogenous angiogenesis inhibitor initially identified in vascular endothelial cells. This 43-44 kDa protein plays a critical role in negative feedback regulation of blood vessel formation by suppressing endothelial cell proliferation and migration. Unlike classical angiogenesis inhibitors that target VEGF signaling, VASH1 operates through distinct mechanisms involving tubulin detyrosination and cytoskeletal modulation. Its expression is induced by pro-angiogenic factors like VEGF and FGF2. creating a self-limiting system for vascular growth.
Recombinant VASH1 protein is typically produced in eukaryotic expression systems (e.g., HEK293 cells) to ensure proper post-translational modifications. The active form often requires co-expression with its binding partner small vasohibin-binding protein (SVBP), which stabilizes VASH1 and enhances its enzymatic activity. Structural studies reveal two conserved domains: an N-terminal domain essential for interaction with SVBP, and a C-terminal domain containing catalytic residues critical for its carboxypeptidase-like activity.
Research applications of recombinant VASH1 span tumor biology, ocular diseases, and tissue engineering. In cancer studies, it suppresses tumor angiogenesis by remodeling immature vasculature in tumor microenvironments. Its anti-angiogenic properties are also investigated for treating diabetic retinopathy and age-related macular degeneration. Pharmaceutical development focuses on its potential as a therapeutic agent with fewer side effects compared to VEGF-targeting drugs.
Validation of recombinant VASH1 functionality typically involves endothelial tube formation assays and tubulin detyrosination tests. Current challenges include optimizing its stability and delivery methods for clinical applications. Emerging evidence suggests additional roles in immune regulation and neuronal development, expanding its potential therapeutic relevance beyond vascular biology.
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