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Mouse Anti-LIMK1 Recombinant Antibody (CBYJL-1713) (CBMAB-L1598-YJ)

Provided herein is a Mouse monoclonal antibody, which binds to Lim Domain Kinase 1 (LIMK1). The antibody can be used for immunoassay techniques, such as ELISA, IHC, WB.
See all LIMK1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYJL-1713
Antibody Isotype
IgG
Application
ELISA, IHC, WB

Basic Information

Immunogen
Partial recombinant protein of human LIMK-1 (aa 548-648) with a GST tag.
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
PBS, pH 7.2
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 548-648

Target

Full Name
LIMK1
Introduction
There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved 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. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. LIMK1 also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms. Diseases associated with LIMK1 include Williams-Beuren Syndrome and Supravalvular Aortic Stenosis. Among its related pathways are Cytoskeleton remodeling Regulation of actin cytoskeleton by Rho GTPases and Apoptotic Pathways in Synovial Fibroblasts.
Entrez Gene ID
3984
UniProt ID
P53667
Alternative Names
LIMK; LIMK-1
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).
Isoform 3
Has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).
Biological Process
Actin cytoskeleton organizationManual Assertion Based On ExperimentIBA:GO_Central
Fc-gamma receptor signaling pathway involved in phagocytosisTAS:Reactome
Negative regulation of ubiquitin-protein transferase activityManual Assertion Based On ExperimentIDA:BHF-UCL
Nervous system developmentManual Assertion Based On ExperimentTAS:ProtInc
Positive regulation of actin filament bundle assemblyManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of axon extensionISS:UniProtKB
Positive regulation of stress fiber assemblyManual Assertion Based On ExperimentIBA:GO_Central
Protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Rho protein signal transductionManual Assertion Based On ExperimentTAS:ProtInc
Signal transductionManual Assertion Based On ExperimentTAS:ProtInc
Cellular Location
Cytoplasm
Nucleus
Cytoplasm, cytoskeleton
Cell projection, lamellipodium
Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner.
Involvement in disease
LIMK1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.
PTM
Autophosphorylated. Phosphorylated on Thr-508 by ROCK1 and PAK1, resulting in activation. Phosphorylated by PAK4 which increases the ability of LIMK1 to phosphorylate cofilin. Phosphorylated at Ser-323 by MAPKAPK2 during activation of VEGFA-induced signaling, which results in activation of LIMK1 and promotion of actin reorganization, cell migration, and tubule formation of endothelial cells. Dephosphorylated and inactivated by SSH1. Phosphorylated by CDC42BP.
Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF6 leads to proteasomal degradation through the 26S proteasome, modulating LIMK1 levels in the growth cone and its effect on axonal outgrowth. Also polyubiquitinated by RLIM (By similarity).

Villalonga, E., Mosrin, C., Normand, T., Girardin, C., Serrano, A., Žunar, B., ... & Vallée, B. (2023). LIM Kinases, LIMK1 and LIMK2, Are Crucial Node Actors of the Cell Fate: Molecular to Pathological Features. Cells, 12(5), 805.

Collins, R., Lee, H., Jones, D. H., Elkins, J. M., Gillespie, J. A., Thomas, C., ... & Foley, D. W. (2022). Comparative analysis of small-molecule LIMK1/2 inhibitors: chemical synthesis, biochemistry, and cellular activity. Journal of Medicinal Chemistry, 65(20), 13705-13713.

Kang, X., Li, W., Liu, W., Liang, H., Deng, J., Wong, C. C., ... & Ng, E. K. W. (2021). LIMK1 promotes peritoneal metastasis of gastric cancer and is a therapeutic target. Oncogene, 40(19), 3422-3433.

Lu, G., Zhou, Y., Zhang, C., & Zhang, Y. (2021). Upregulation of LIMK1 is correlated with poor prognosis and immune infiltrates in lung adenocarcinoma. Frontiers in genetics, 12, 671585.

Zhang, M., Wang, R., Tian, J., Song, M., Zhao, R., Liu, K., ... & Lee, M. H. (2021). Targeting LIMK1 with luteolin inhibits the growth of lung cancer in vitro and in vivo. Journal of cellular and molecular medicine, 25(12), 5560-5571.

Li, Z. F., Yao, Y. D., Zhao, Y. Y., Liu, Y., Liu, Z. H., Hu, P., & Zhu, Z. R. (2020). Effects of PAK4/LIMK1/Cofilin‐1 signaling pathway on proliferation, invasion, and migration of human osteosarcoma cells. Journal of clinical laboratory analysis, 34(9), e23362.

Salah, E., Chatterjee, D., Beltrami, A., Tumber, A., Preuss, F., Canning, P., ... & Mathea, S. (2019). Lessons from LIMK1 enzymology and their impact on inhibitor design. Biochemical Journal, 476(21), 3197-3209.

Henderson, B. W., Greathouse, K. M., Ramdas, R., Walker, C. K., Rao, T. C., Bach, S. V., ... & Herskowitz, J. H. (2019). Pharmacologic inhibition of LIMK1 provides dendritic spine resilience against β-amyloid. Science signaling, 12(587), eaaw9318.

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For research use only. Not intended for any clinical use.

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