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L2290

Sigma-Aldrich

Anti-LIM Kinase 1 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinônimo(s):

Anti-LIMK1

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.44

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

IgG fraction of antiserum

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

reatividade de espécies

human, mouse, rat

técnica(s)

microarray: suitable
western blot: 1:2,000 using a cytosolic fraction of rat brain.

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... LIMK1(3984)
mouse ... Limk1(16885)
rat ... Limk1(65172)

Descrição geral

LIM Domain Kinase 1 (LIMK1) belongs to the LIMK family of serine/threonine protein kinases. LIMK1 shares about 50% sequence identity with LIMK2. LIMK1 contains two N-terminal LIM domains, an internal PDZ (post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1)) domain and a C-terminal kinase domain.

Imunogênio

Synthetic peptide corresponding to the C-terminus of mouse LIMK1 (amino acids 627-647 or 613-633 of the alternatively spliced forms of LIMK1), conjugated to KLH
This sequence is identical in rat LIMK1 and highly conserved (single amino acid substitution) in human LIMK1. It is not found in the LIMK2 isoform.

Aplicação

Anti-LIM Kinase 1 antibody is suitable for use in microarrays, protein densitometric assays (1:1000 using BPAE cell extracts ) and western blot (1:100, 000 using MDA-MB-231 cell lysates ).

Ações bioquímicas/fisiológicas

LIMK1 phosphorylates cofilin specifically at Serine 3. This inactivates its F-actin depolymerizing activity and leads to actin reorganization and accumulation of actin filaments. LIMK1 mRNA is highly expressed in the developing nervous system, heart and gut, and in adult brain and spinal cord, suggesting a role for LIMK-1 during neuronal cell differentiation. LIMK1 is localized in the presynaptic nerve ending during the synapse maturation event. LIMK1 also exhibits mitosis-specific activation.

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Exoneração de responsabilidade

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Tissue specific characterisation of Lim-kinase 1 expression during mouse embryogenesis
Lindstrom NO, et al.
Gene Expression Patterns, 11(3-4), 221-232 (2011)
Mitosis-specific activation of LIM motif-containing protein kinase and roles of cofilin phosphorylation and dephosphorylation in mitosis
Amano T, et al.
The Journal of biological chemistry, 277(24), 22093-22102 (2002)
J Y Wang et al.
The Journal of comparative neurology, 416(3), 319-334 (1999-12-22)
LIM kinase 1 (LIMK1) is a cytoplasmic protein kinase that is highly expressed in neurons. In transfected cells, LIMK1 binds to the cytoplasmic tail of neuregulins and regulates the breakdown of actin filaments. To identify potential functions of LIMK1 in
Patricia Castañeda et al.
Journal of neuroscience research, 93(10), 1476-1491 (2015-05-27)
Chronic stress promotes cognitive impairment and dendritic spine loss in hippocampal neurons. In this animal model of depression, spine loss probably involves a weakening of the interaction between pre- and postsynaptic cell adhesion molecules, such as N-cadherin, followed by disruption
Zoe M Goeckeler et al.
The Journal of biological chemistry, 280(38), 33083-33095 (2005-08-02)
This study determined the effects of increased intracellular cAMP and cAMP-dependent protein kinase activation on endothelial cell basal and thrombin-induced isometric tension development. Elevation of cAMP and maximal cAMP-dependent protein kinase activation induced by 10 microm forskolin, 40 microm 3-isobutyl-1-methylxanthine

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