纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LPXN |
Uniprot No | O60711 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-386aa |
氨基酸序列 | MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ DNTSPLPAQL VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL TEMQAKVAVR ADAGKKHLPD KQDHKASLDS MLGGLEQELQ DLGIATVPKG HCASCQKPIA GKVIHALGQS WHPEHFVCTH CKEEIGSSPF FERSGLAYCP NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC GEVFGAEGFH EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP EHFVCAFCLT QLSKGIFREQ NDKTYCQPCF NKLFPL |
预测分子量 | 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LPXN(Leupaxin)重组蛋白的3篇参考文献示例:
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1. **文献名称**: *"Leupaxin interacts with paxillin to regulate adhesion-induced tyrosine phosphorylation and cell migration"*
**作者**: W. Li et al.
**摘要**: 该研究通过重组表达人源LPXN蛋白,揭示了其与paxillin的相互作用机制,并证明其在细胞黏附和迁移过程中对酪氨酸磷酸化的调控作用,为理解癌症转移提供了分子基础。
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2. **文献名称**: *"Recombinant Leupaxin expression in prostate cancer cells modulates integrin signaling and invasiveness"*
**作者**: S. R. Thomas et al.
**摘要**: 研究利用重组LPXN蛋白探究其在前列腺癌细胞中的功能,发现其通过整合素信号通路增强肿瘤细胞侵袭性,提示LPXN可能成为癌症治疗的潜在靶点。
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3. **文献名称**: *"Structural and functional characterization of the Leupaxin PDZ domains"*
**作者**: M. K. Lee et al.
**摘要**: 该研究通过重组表达和晶体学分析,解析了LPXN蛋白的PDZ结构域三维结构,并阐明其在细胞骨架蛋白相互作用中的关键作用,为设计靶向药物提供结构依据。
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(注:以上文献为示例性内容,实际引用时需核对真实来源。)
**Background of LPXN Recombinant Protein**
Leupaxin (LPXN), a member of the paxillin protein family, is a cytoskeletal adaptor protein involved in cell adhesion, migration, and signal transduction. It is primarily expressed in immune cells, endothelial cells, and certain cancer cells. Structurally, LPXN contains four tandem leucine-rich LD motifs and LIM domains, enabling interactions with focal adhesion kinases (e.g., FAK, PYK2) and SRC-family kinases. These interactions facilitate the assembly of signaling complexes at focal adhesions, linking extracellular matrix signals to intracellular pathways that regulate cytoskeletal dynamics and gene expression.
LPXN gained attention for its role in modulating integrin-mediated signaling, which influences cell motility and survival. Studies highlight its involvement in cancer progression, particularly in metastasis, where LPXN overexpression correlates with enhanced tumor cell invasion and poor prognosis. Additionally, LPXN regulates immune responses by affecting leukocyte adhesion and trafficking, suggesting potential roles in inflammatory diseases.
Recombinant LPXN protein is produced using expression systems like *E. coli* or mammalian cells, ensuring high purity and activity for research applications. It serves as a critical tool for studying LPXN’s biochemical properties, ligand-binding interactions, and downstream signaling mechanisms *in vitro*. Researchers also utilize it to develop inhibitors targeting LPXN-associated pathways for therapeutic purposes, such as anti-cancer or anti-inflammatory drugs.
The development of LPXN recombinant protein has advanced understanding of its structural-functional relationships and disease relevance, positioning it as a promising biomarker and therapeutic target in oncology and immunology. Ongoing research aims to unravel its tissue-specific roles and exploit its regulatory networks for clinical interventions.
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