| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LASP1 |
| Uniprot No | Q14847 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-261aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMNPNCARCGKIVYPTEKVNCLDKFWH KACFHCETCKMTLNMKN YKGYEKKPYCNAHYPKQSFTMVADTPENLRL KQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRI KKTQDQISNIKY HEEFEKSRMGPSGGEGMEPERRDSQDGSSYRRPLEQQQPHHIPTSAPVYQ QPQQQ PVAQSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDE VSFQDGDTIVNVQQIDDGWMYGTV ERTGDTGMLPANYVEAI |
| 预测分子量 | 32 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LASP1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *LASP1. a novel LIM-protein, is upregulated in human breast cancer and promotes proliferation and metastasis*
**作者**: Grünewald TG, et al.
**摘要**: 本研究通过重组LASP1蛋白的体外实验，发现其通过与zyxin和PDPK1等蛋白相互作用，激活PI3K/AKT信号通路，促进乳腺癌细胞增殖、迁移和侵袭，揭示了LASP1在肿瘤进展中的分子机制。
2. **文献名称**: *Recombinant LASP1 protein enhances cell migration via regulating focal adhesion dynamics*
**作者**: Zhang Y, et al.
**摘要**: 利用重组LASP1蛋白进行功能研究，发现其通过结合细胞骨架蛋白(如F-actin和vinculin)，调控黏着斑的形成与解聚，从而增强肝癌细胞迁移能力，为靶向LASP1的抗转移治疗提供依据。
3. **文献名称**: *Structural and functional characterization of the LASP1 LIM domain using recombinant protein expression*
**作者**: Duvall-Erne S, et al.
**摘要**: 通过重组表达LASP1的LIM结构域蛋白，解析其晶体结构并验证其与细胞骨架蛋白的互作界面，证实该结构域对LASP1定位至伪足尖端及细胞极性调控的关键作用。
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**备注**：以上文献信息为模拟示例，实际研究中建议通过PubMed或专业数据库核对具体文献。
LASP1 (LIM and SH3 protein 1) is a multifunctional adaptor protein first identified in 1995 from human breast cancer and placental cDNA libraries. It belongs to the LIM protein family, characterized by the presence of LIM domains (zinc-binding motifs involved in protein-protein interactions) and an Src homology 3 (SH3) domain. Structurally, LASP1 contains an N-terminal LIM domain, a central nuclear localization signal, and a C-terminal SH3 domain, enabling interactions with cytoskeletal components, signaling molecules, and nucleic acids. The gene encoding LASP1 is located on chromosome 17q12. a region frequently amplified in cancers.
Functionally, LASP1 regulates cell migration, proliferation, and adhesion by interacting with actin-binding proteins (e.g., zyxin, palladin) and signaling pathways (e.g., FAK, Src). It localizes to dynamic actin-rich structures like focal adhesions and lamellipodia, influencing cytoskeletal remodeling. Overexpression of LASP1 is implicated in cancer progression, particularly in breast, colorectal, and hepatocellular carcinomas, where it promotes metastasis and correlates with poor prognosis. It also plays roles in non-cancer pathologies, including cardiovascular and inflammatory diseases.
Recombinant LASP1 proteins are engineered using expression systems (e.g., E. coli, mammalian cells) for functional studies. These purified proteins retain domains critical for binding partners and are utilized to investigate LASP1's molecular mechanisms, validate interactomes, and screen therapeutic inhibitors. Tagged versions (e.g., His, GST) facilitate purification and detection. Research on recombinant LASP1 has advanced understanding of its dual roles in physiological processes and disease, highlighting its potential as a diagnostic marker or therapeutic target. However, its nuclear functions and context-dependent regulation remain active areas of exploration.
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