| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VASP |
| Uniprot No | P50552 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-343aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSD |
| 预测分子量 | 38 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VASP重组蛋白的3篇代表性文献摘要简述：
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1. **文献名称**: *The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins*
**作者**: Reinhard, M., et al.
**摘要**: 本研究利用重组表达的VASP蛋白，揭示了其与profilin(一种肌动蛋白结合蛋白)的直接相互作用，阐明了VASP在调节细胞骨架动态中的分子机制。
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2. **文献名称**: *Structural basis for the actin-binding function of VASP*
**作者**: Bachmann, C., et al.
**摘要**: 通过重组VASP蛋白的晶体结构分析，确定了其EVH2结构域与G-actin结合的关键区域，解释了VASP促进肌动蛋白成核和纤维形成的结构基础。
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3. **文献名称**: *Regulation of VASP phosphorylation in platelet activation*
**作者**: Smolenski, A., et al.
**摘要**: 利用重组VASP蛋白研究cAMP/cGMP依赖性蛋白激酶对其磷酸化的调控，表明磷酸化位点(Ser157/Ser239)影响VASP在血小板聚集中的抑制作用。
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*注：以上文献信息为简化示例，实际引用需核对具体来源及发表年份。*
Vasodilator-Stimulated Phosphoprotein (VASP) is a key cytoskeletal regulatory protein involved in actin filament dynamics, cell adhesion, and motility. Belonging to the Ena/VASP family, it plays a critical role in coordinating actin polymerization and cellular responses to extracellular signals. Structurally, VASP contains conserved domains: an N-terminal EVH1 domain for protein-protein interactions, a central proline-rich region, and a C-terminal EVH2 domain that binds actin and facilitates filament assembly. Its activity is modulated by phosphorylation, particularly in response to cyclic nucleotide signaling pathways (e.g., cAMP/cGMP), linking cellular motility to physiological stimuli.
Recombinant VASP proteins are engineered using heterologous expression systems (e.g., E. coli, insect cells) to study structure-function relationships and molecular mechanisms. These recombinant constructs often include affinity tags (e.g., GST, His-tag) for purification and tracking. Researchers utilize them to dissect VASP's role in actin-driven processes, such as lamellipodia formation, focal adhesion turnover, and cell migration. Notably, VASP dysfunction is implicated in pathological conditions, including cancer metastasis, vascular remodeling disorders, and impaired wound healing.
The development of recombinant VASP has advanced structural studies (e.g., crystallography, NMR) and biochemical assays, revealing how post-translational modifications or disease-associated mutations alter its activity. It also enables high-throughput screening for therapeutic compounds targeting actin-related pathologies. Current research focuses on VASP's interplay with other cytoskeletal regulators (e.g., Arp2/3 complex, formins) and its potential as a biomarker or therapeutic target in cardiovascular diseases and invasive cancers.
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