| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIMCH1 |
| Uniprot No | Q9UPQ0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1083aa |
| 氨基酸序列 | MACPALGLEALQPLQPEPPPEPAFSEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNIILFLRGCKELGLKESQLFDPSDLQDTSNRVTVKSLDYSRKLKNVLVTIYWLGKAANSCTSYSGTTLNLKEFEGLLAQMRKDTDDIESPKRSIRDSGYIDCWDSERSDSLSPPRHGRDDSFDSLDSFGSRSRQTPSPDVVLRGSSDGRGSDSESDLPHRKLPDVKKDDMSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEYRKSWSTATSPLGGERPFRYGPRTPVSDDAESTSMFDMRCEEEAAVQPHSRARQEQLQLINNQLREEDDKWQDDLARWKSRRRSVSQDLIKKEEERKKMEKLLAGEDGTSERRKSIKTYREIVQEKERRERELHEAYKNARSQEEAEGILQQYIERFTISEAVLERLEMPKILERSHSTEPNLSSFLNDPNPMKYLRQQSLPPPKFTATVETTIARASVLDTSMSAGSGSPSKTVTPKAVPMLTPKPYSQPKNSQDVLKTFKVDGKVSVNGETVHREEEKERECPTVAPAHSLTKSQMFEGVARVHGSPLELKQDNGSIEINIKKPNSVPQELAATTEKTEPNSQEDKNDGGKSRKGNIELASSEPQHFTTTVTRCSPTVAFVEFPSSPQLKNDVSEEKDQKKPENEMSGKVELVLSQKVVKPKSPEPEATLTFPFLDKMPEANQLHLPNLNSQVDSPSSEKSPVMTPQFKFWAWDPEEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQKEVEEEERRYYEEERKIIEDTVVPFTVSSSSADQLSTSSSMTEGSGTMNKIDLGNCQDEKQDRRWKKSFQGDDSDLLLKTRESDRLEEKGSLTEGALAHSGNPVSKGVHEDHQLDTEAGAPHCGTNPQLAQDPSQNQQTSNPTHSSEDVKPKTLPLDKSINHQIESPSERRKKSPREHFQAGPFSPCSPTPPGQSPNRSISGKKLCSSCGLPLGKGAAMIIETLNLYFHIQCFRCGICKGQLGDAVSGTDVRIRNGLLNCNDCYMRSRSAGQPTTL |
| 预测分子量 | 121,8 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条与LIMCH1重组蛋白相关的参考文献(内容基于真实文献方向概括，部分信息为模拟简化版)：
1. **文献名称**：*LIMCH1 regulates nonmuscle myosin II activity and mechanotransduction in cell spreading*
**作者**：Smith A, et al.
**摘要**：研究通过重组LIMCH1蛋白体外实验，发现其通过结合非肌肉肌球蛋白II(NMII)调控细胞机械信号响应，揭示其在细胞铺展和迁移中的分子机制。
2. **文献名称**：*Structural insights into the autoinhibition and phosphorylation-dependent activation of LIMCH1*
**作者**：Chen L, et al.
**摘要**：利用重组LIMCH1蛋白进行结构解析，阐明其自抑制构象及磷酸化激活机制，为理解其在细胞骨架动态调控中的作用提供结构基础。
3. **文献名称**：*LIMCH1 deficiency disrupts focal adhesion signaling and leads to myopathy in vivo*
**作者**：Wang Y, et al.
**摘要**：通过重组蛋白互作实验，证实LIMCH1与黏着斑蛋白(如Paxillin)结合，调控黏着斑信号通路，缺失可导致体内肌肉病理表型。
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**注**：以上为示例性内容，实际文献需通过PubMed/Google Scholar检索关键词“LIMCH1 recombinant”或结合具体研究方向筛选。如需真实文献，可提供更具体的研究背景进一步协助查询。
LIMCH1 (LIM and calponin homology domains-containing protein 1) is a cytoskeleton-associated protein implicated in regulating cellular mechanical properties and actin dynamics. It belongs to the LIM protein family, characterized by the presence of LIM domains, which are zinc-binding motifs that mediate protein-protein interactions. The human LIMCH1 gene encodes a multi-domain protein containing two N-terminal LIM domains and a C-terminal calponin homology (CH) domain. These structural features suggest its involvement in bridging signaling molecules with the actin cytoskeleton, potentially influencing cell adhesion, migration, and mechanotransduction.
Recombinant LIMCH1 protein is typically produced through heterologous expression systems (e.g., E. coli or mammalian cells) to study its biochemical functions and interactions. Researchers utilize it to investigate its role in binding actin filaments, modulating actomyosin contractility, and interacting with Rho GTPase signaling pathways. Studies have linked LIMCH1 to cellular responses to mechanical stress and the maintenance of cell shape, with emerging evidence connecting its dysregulation to cardiovascular diseases and cancer metastasis. For instance, LIMCH1 deficiency has been associated with impaired smooth muscle cell contraction and abnormal vascular development in model organisms.
The production of recombinant LIMCH1 enables structural analysis, antibody development, and high-throughput screening for potential therapeutic targets. Despite progress, its precise molecular mechanisms remain partially understood, particularly regarding how its LIM domains coordinate with the CH domain to regulate cytoskeletal remodeling. Current research focuses on elucidating its tissue-specific functions and pathological relevance, leveraging recombinant protein tools to dissect its role in cellular biomechanics and disease progression.
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