Product: LIMK1 Antibody
Catalog: AF6345
Description: Rabbit polyclonal antibody to LIMK1
Application: WB IF/ICC
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 70kDa; 73kD(Calculated).
Uniprot: P53667
RRID: AB_2835201

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Product Info

WB 1:500-1:2000, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
LIMK1 Antibody detects endogenous levels of total LIMK1.
Cite Format: Affinity Biosciences Cat# AF6345, RRID:AB_2835201.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


EC; LIM domain kinase 1; LIM motif-containing protein kinase; LIMK; LIMK-1; limk1; LIMK1_HUMAN;



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.

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 likely to be a component of an intracellular signaling pathway and may be involved in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Two splice variant have been identified.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P53667 As Substrate

Site PTM Type Enzyme
S58 Phosphorylation
S210 Phosphorylation
K214 Ubiquitination
T229 Phosphorylation
T253 Phosphorylation
T270 Phosphorylation
S274 Phosphorylation
S286 Phosphorylation
S287 Phosphorylation
S296 Phosphorylation
S298 Phosphorylation
S302 Phosphorylation
S307 Phosphorylation O14965 (AURKA)
S310 Phosphorylation Q16539 (MAPK14)
S313 Phosphorylation
R320 Methylation
S323 Phosphorylation P49137 (MAPKAPK2)
S337 Phosphorylation
K368 Ubiquitination
T508 Phosphorylation Q9NQU5 (PAK6) , Q13464 (ROCK1) , Q13153 (PAK1) , Q16566 (CAMK4) , O14965 (AURKA)
S534 Phosphorylation
S637 Phosphorylation

PTMs - P53667 As Enzyme

Substrate Site Source
P23528 (CFL1) S3 Uniprot
P50281 (MMP14) Y573 Uniprot
P53667-1 (LIMK1) S298 Uniprot
P53667-1 (LIMK1) S310 Uniprot
P60981 (DSTN) S3 Uniprot
Q9Y281-1 (CFL2) S3 Uniprot

Research Backgrounds


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. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. 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. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development.

Has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).


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).

Subcellular Location:

Cytoplasm. Nucleus. Cytoplasm>Cytoskeleton. Cell projection>Lamellipodium.
Note: Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

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.

Subunit Structure:

Interacts (via LIM domain) with the cytoplasmic domain of NRG1. Interacts with NISCH. Interacts with RLIM and RNF6 (By similarity). Self-associates to form homodimers. Interacts with HSP90AA1; this interaction promotes LIMK1 dimerization and subsequent transphosphorylation. Interacts with CDKN1C. Interacts with SSH1. Interacts with ROCK1. Interacts (via LIM zinc-binding domains) with FAM89B/LRAP25 (via LRR repeat). Forms a tripartite complex with CDC42BPA, CDC42BPB and FAM89B/LRAP25 (By similarity).


Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Research Fields

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Organismal Systems > Development > Axon guidance.   (View pathway)

· Organismal Systems > Immune system > Fc gamma R-mediated phagocytosis.   (View pathway)


1). The p75 neurotrophin receptor as a novel intermediate in L-dopa-induced dyskinesia in experimental Parkinson's disease. Experimental Neurology, 2021 (PubMed: 33971218) [IF=5.3]

Application: WB    Species: Rat    Sample: striatal tissue

Fig. 3. TH, ΔFosB, p75NTR and Iba1 expression in sham, PD and LID rats. (A-E) TH, ΔFosB, p75NTR, ROCK2, total and phosphor-LIMK1, total and phosphor-Cofilin, and Iba1 protein levels determined by WB from ipsilateral striatal extracts obtained from sham, PD and LID rats and actin as loading control. Data are mean ± SEM (4 striata/group) (One-way ANOVA followed by Sidak’s multiple comparisons test). *P < 0.05, ***P < 0.001 vs sham lesioned group lesioned striatal tissue; ## P < 0.05,### P < 0.001 vs 6-OHDA lesioned group lesioned striatal tissue.) Abbreviations: PD, Parkinson’s disease; LID, L-dopa-induced dyskinesia; p75NTR, p75 neurotrophic receptor; WB, Western Blot; TH, Tyrosine Hydroxylase.

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