LIM Kinase 1 (LIMK1) Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
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Primary Accession | P53667 |
Other Accession | P53669, P53668 |
Reactivity | Human |
Predicted | Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 72585 Da |
Antigen Region | 1-30 aa |
Gene ID | 3984 |
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Other Names | LIM domain kinase 1, LIMK-1, LIMK1, LIMK |
Target/Specificity | This LIM Kinase 1 (LIMK1) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human LIM Kinase 1 (LIMK1). |
Dilution | WB~~1:1000 IHC-P~~1:50~100 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | LIM Kinase 1 (LIMK1) Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | LIMK1 |
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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
LIMK1, a member of the Ser/Thr protein kinase family, may be a component of an intracellular signaling pathway and may be involved in brain development. It phosphorylates and inactivates the actin binding/depolymerizing factor cofilin and induces actin cytoskeletal changes. The LIM domain interacts with the cytoplasmic domain of NRG1, and this cytoplasmic protein also binds ROCK1, whic phosphorylates LIMK1 on serine and/or threonine residues. Highest expression occurs in both adult and fetal nervous systems. It is detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex, and is expressed to a lesser extent in heart and skeletal muscle. Haploinsufficiency of LIMK1 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS), a rare developmental disorder. It is a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23. This protein contains 2 LIM zinc-binding domains and 1 PDZ/DHR domain.
References
Ohashi, K., et al., J. Biol. Chem. 275(5):3577-3582 (2000).
Maekawa, M., et al., Science 285(5429):895-898 (1999).
Edwards, D.C., et al., J. Biol. Chem. 274(16):11352-11361 (1999).
Osborne, L.R., et al., Genomics 36(2):328-336 (1996).
Frangiskakis, J.M., et al., Cell 86(1):59-69 (1996).
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