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Key Documents

SAB4501949

Sigma-Aldrich

Anti-MYPT1 antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

MBS, Myosin phosphatase target subunit 1, PPP1R12A

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About This Item

Numéro MDL:
MFCD04118624
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 115 kDa

Espèces réactives

human, mouse, rat

Concentration

~1 mg/mL

Technique(s)

ELISA: 1:5000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

Numéro d'accès NCBI

O14974

Numéro d'accès UniProt

O14974

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PPP1R12A(4659)

Catégories apparentées

Description générale

Anti-MYPT1 Antibody detects endogenous levels of total MYPT1 protein. Myosin phosphatase target subunit 1 (MYPT1) is also known as protein phosphatase 1 regulatory subunit 12A (PPP1R12A). It is the regulatory subunit of the myosin light chain phosphatase. MYPT1 has a molecular weight of 130 kDa. The gene encoding this protein is localized on human chromosome 12q21.2.

Immunogène

The antiserum was produced against synthesized peptide derived from human MYPT1.

Immunogen Range: 621-670

Actions biochimiques/physiologiques

Myosin phosphatase target subunit 1 (MYPT1) has a role in the modulation of the myosin light chain phosphatase through its multiple phosphorylation sites. It aids in the interaction of protein phosphatase-1 catalytic subunit δ (PP1C) with myosin filaments. MYPT1 acts as an antagonist of polo-like kinase-1 (PLK1) and has a role in regulating mitosis.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Gene trap as a tool for genome annotation and analysis of X chromosome inactivation in human embryonic stem cells.
Dhara S K and Benvenisty N
Nucleic Acids Research, 32(13), 3995-4002 (2004)
Myosin phosphatase-targeting subunit 1 controls chromatid segregation.
Matsumura F, et al.
The Journal of Biological Chemistry, 286(12), 10825-10833 (2011)
Mukta Khasnis et al.
Biochemistry, 53(16), 2701-2709 (2014-04-10)
The myosin light chain phosphatase (MLCP) is a cytoskeleton-associated protein phosphatase-1 (PP1) holoenzyme and a RhoA/ROCK effector, regulating cytoskeletal reorganization. ROCK-induced phosphorylation of the MLCP regulatory subunit (MYPT1) at two sites, Thr696 and Thr853, suppresses the activity, although little is
Ahmed Aburima et al.
Blood, 122(20), 3533-3545 (2013-10-09)
Cyclic adenosine monophosphate (cAMP)-dependent signaling modulates platelet shape change through unknown mechanisms. We examined the effects of cAMP signaling on platelet contractile machinery. Prostaglandin E1 (PGE1)-mediated inhibition of thrombin-stimulated shape change was accompanied by diminished phosphorylation of myosin light chain
Daisuke Mori et al.
Journal of pharmacological sciences, 125(4), 394-405 (2014-07-30)
Intestinal inflammation causes disorder in bowel motility. Th17 cytokines are involved in intestinal inflammation. To understand the role of interleukin (IL)-17 in intestinal motility, we examined effects of IL-17A on contractile activities of organ-cultured ileum. Rat ileal smooth muscle strips
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