M6068
Anti-phospho-Myosin Light Chain (pSer19) antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
Synonyme(s) :
Anti-MLC
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About This Item
Produits recommandés
Source biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous glycerol solution
Espèces réactives
human (predicted), chicken
Technique(s)
western blot: 1:1,000 using chicken gizzard myosin II phosphorylated in vitro by PAK
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
phosphorylation (pSer19)
Informations sur le gène
human ... MYL1(4632)
Description générale
Myosin light chains belongs to the calmodulin (CaM) gene family.
Rabbit polyclonal anti-phospho-Myosin Light Chain (pSer19) antibody detects chicken MLC. Results show that reactivity with the antibody requires phosphorylation of MLC by active kinase, and that only the peptide corresponding to MLC (pSer19) blocks the antibody signal, thereby demonstrating the specificity of the antibody. Human (100% homologous) has not been tested, but is expected to react.
Immunogène
synthetic phosphopeptide derived from the region of chicken MLC that contains serine 19 (serine 20 including the initiating methionine). Human (100% homologous) has not been tested, but is expected to cross-react.
Application
Anti-phospho-Myosin Light Chain (pSer19) antibody produced in rabbit has been used in the detection of phosphorylated myosin: in human lung fibroblasts and avian lens cells by immunoblotting by immunohistochemical detection in rabbit aorta samplesby immunofluorescence detection in human submandibular gland tissues
Actions biochimiques/physiologiques
Myosin light chain is a subunit of the conventional myosins, e.g., myosin II. In smooth muscle and nonmuscle cells, conventional myosins mediate a wide variety of contractile events including cytokinesis, cell motility, and smooth muscle contraction. MLC is phosphorylated by multiple serine-threonine kinases such as Rho-kinase and PAK, however, myosin light chain kinase (MLCK) acts as the primary kinase. Contractile activity of conventional myosins is regulated by phosphorylation of MLC on several residues. Phosphorylation of serine 19, the major phosphorylation site and the preferred site for MLCK, activates myosin motor activity under physiological conditions.
Myosin light chains functions to maintain integrity of myosin protein. Mutations in the myosin light chain is implicated in familial hypertrophic cardiomyopathy.
Forme physique
Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3 (± 0.1), 50% glycerol with 1.0 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.
Clause de non-responsabilité
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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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Shuichi Asano et al.
Physiological reports, 5(9) (2017-05-17)
In patients with pulmonary diseases such as idiopathic pulmonary fibrosis and severe acute respiratory distress syndrome, progressive pulmonary fibrosis is caused by dysregulated wound healing via activation of fibroblasts after lung inflammation or severe damage. Migration of fibroblasts toward the
Myosin essential light chain in health and disease
Hernandez OM, et al.
American Journal of Physiology. Heart and Circulatory Physiology, 292(4), H1643-H1654 (2007)
Myosin light chain kinase inhibitor ML7 improves vascular endothelial dysfunction via tight junction regulation in a rabbit model of atherosclerosis
Cheng X, et al.
Molecular Medicine Reports, 12(3), 4109-4116 (2015)
Dorian Obino et al.
Cell reports, 25(11), 3110-3122 (2018-12-13)
Complete activation of B cells relies on their capacity to extract tethered antigens from immune synapses by either exerting mechanical forces or promoting their proteolytic degradation through lysosome secretion. Whether antigen extraction can also be tuned by local cues originating
Myosin light chains: teaching old dogs new tricks
Heissler SM and Sellers JR
Bioarchitecture, 4(6), 169-188 (2014)
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