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Phospho-LIMK1(Thr508)) Antibody Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P53667 |
|---|---|
| Clone Names | 100720001 |
| Gene ID | 3984 |
|---|---|
| Other Names | LIM domain kinase 1, LIMK-1, LIMK1, LIMK |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | LIMK1 |
|---|---|
| Synonyms | LIMK |
| Function | Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11832213, PubMed:12807904, PubMed:15660133, PubMed:16230460, PubMed:18028908, PubMed:22328514, PubMed:23633677). Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop (PubMed:10436159). LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly (PubMed:18028908). Stimulates axonal outgrowth and may be involved in brain development (PubMed:18028908). |
| Cellular Location | Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P53668} Note=Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:P53668} |
| Tissue Location | Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle |
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Provided below are standard protocols that you may find useful for product applications.
Background
There are approximately 40 known eukaryotic LIM proteins,so named for the LIM domains they contain. LIM domains are highlyconserved cysteine-rich structures containing 2 zinc fingers.Although zinc fingers usually function by binding to DNA or RNA,the LIM motif probably mediates protein-protein interactions. LIMkinase-1 and LIM kinase-2 belong to a small subfamily with a uniquecombination of 2 N-terminal LIM motifs and a C-terminal proteinkinase domain. LIMK1 is likely to be a component of anintracellular signaling pathway and may be involved in braindevelopment. LIMK1 hemizygosity is implicated in the impairedvisuospatial constructive cognition of Williams syndrome. [providedby RefSeq].
References
There are approximately 40 known eukaryotic LIM proteins,so named for the LIM domains they contain. LIM domains are highlyconserved cysteine-rich structures containing 2 zinc fingers.Although zinc fingers usually function by binding to DNA or RNA,the LIM motif probably mediates protein-protein interactions. LIMkinase-1 and LIM kinase-2 belong to a small subfamily with a uniquecombination of 2 N-terminal LIM motifs and a C-terminal proteinkinase domain. LIMK1 is likely to be a component of anintracellular signaling pathway and may be involved in braindevelopment. LIMK1 hemizygosity is implicated in the impairedvisuospatial constructive cognition of Williams syndrome. [providedby RefSeq].
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