LIMK1 (C-terminus) Peptide | LIMK1 peptide

LIMK1 (C-terminus) Peptide

Cat. Num. AAA474011

• Gene Names: LIMK1; LIMK; LIMK-1
• Synonyms: LIMK1 (C-terminus) Peptide; LIMK1 peptide

• Specificity: The peptide is specifically recognized by LIMK1 (Cterminus) antibody (LP1831) in ELISA, and has been shown to block the reactivity of LP1831 in Western blot and immunocytochemistry.
• Form/Format: Blocking Peptide is supplied in 50ul phosphate-buffered saline and 0.05% sodium azide.
• Sequence: Peptide Sequence: LIMK1 (C-terminus) synthetic peptide corresponding to amino acids at the C-terminus of human LIMK1. This sequence is conserved in rat and mouse LIMK1, and is not found in LIMK2.
• Sequence Length: 647

• Application Notes: ELISA: 50 ng/well; Western Blot: 1:1,000
• Preparation and Storage: Store at -20 degree C. Stable for 1 year.

Related Product Information for LIMK1 peptide

LIM kinases (LIMK1 and LIMK2) are serine/threonine kinases that have two zinc finger motifs, known as LIM motifs, in their aminoterminal regulatory domains. LIM kinases are involved in actin cytoskeletal regulation downstream of Rho-family GTPases, PAKs, and ROCK. PAK1 and ROCK phosphorylate LIMK1 or LIMK2 at the conserved Thr-508 or Thr-505 residues in the activation loop, increasing LIMK activity. In addition, VEGF-induced stress fiber formation has been linked to p38-mediated activation of LIMK through MK-2 phosphorylation of Ser-323. Activated LIM kinases inhibit the actin depolymerization activity of cofilin by phosphorylation at the amino-terminal Ser-3 residue of cofilin. In addition, LIMKs may have a function in the nucleus. It has been shown that the nuclear localization of LIMKs can mediate suppression of Rac/Cdc42-mediated cyclin D1 expression. This effect of LIMKs was independent of cofilin phosphorylation and the regulation of actin dynamics.

References

• Okano, I. et al. (1995) J. Biol. Chem. 270:31321.
• Edwards, D. C. et al. (1999) Nat. Cell Biol. 1:253.
• Kobayashi, M. et al. (2006) EMBOJ 25:713.

NCBI and Uniprot Product Information

• NCBI GI #: 4505001
• NCBI GeneID: 3984
• NCBI Accession #: NP_002305.1
• NCBI GenBank Nucleotide #: NM_002314.2
• UniProt Accession #: P53667; O15283; Q15820; Q15821; Q75MU3; Q9Y5Q1; D3DXF4; D3DXF5; Q59FA3; Q75MU0; Q75MU4
• Molecular Weight: 72454 Da
• NCBI Official Full Name: LIM domain kinase 1 isoform 1
• NCBI Official Synonym Full Names: LIM domain kinase 1
• NCBI Official Symbol: LIMK1
• NCBI Official Synonym Symbols: LIMK; LIMK-1
• NCBI Protein Information: LIM domain kinase 1; OTTHUMP00000160532; OTTHUMP00000211913; LIM motif-containing protein kinase
• UniProt Protein Name: LIM domain kinase 1
• Protein Family: LIM domain kinase
• UniProt Gene Name: LIMK1
• UniProt Synonym Gene Names: LIMK
• UniProt Entry Name: LIMK1_HUMAN

NCBI Description

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. This protein 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.

Uniprot Description

Function: Protein kinase which regulates actin filament dynamics. Phosphorylates and inactivates the actin binding/depolymerizing factor cofilin, thereby stabilizing the actin cytoskeleton. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Ref.4 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.

Subunit structure: Self-associates. The LIM domain interacts with the cytoplasmic domain of NRG1. Binds ROCK1. Interacts with SSH1. Interacts with NISCH

By similarity. Interacts with RLIM and RNF6

By similarity. Interacts with TPPP. Ref.7 Ref.8 Ref.12 Ref.14

Subcellular location: Cytoplasm. Cell projection › growth cone

By similarity Ref.4 Ref.13.

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.

Post-translational modification: Autophosphorylated

By similarity. Ref.8 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19Phosphorylated on serine and/or threonine residues by ROCK1. May be dephosphorylated and inactivated by SSH1. Ref.8 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19Ubiquitinated. '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

Involvement in disease: Note=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.

Sequence similarities: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.Contains 2 LIM zinc-binding domains.Contains 1 PDZ (DHR) domain.Contains 1 protein kinase domain.