Skip to Content
Merck
All Photos(2)

Documents

SAB4501949

Sigma-Aldrich

Anti-MYPT1 antibody produced in rabbit

affinity isolated antibody

Synonym(s):

MBS, Myosin phosphatase target subunit 1, PPP1R12A

Sign Into View Organizational & Contract Pricing
All Photos(2)

About This Item

MDL number:
MFCD04118624
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 115 kDa

species reactivity

human, mouse, rat

concentration

~1 mg/mL

technique(s)

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

NCBI accession no.

O14974

UniProt accession no.

O14974

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PPP1R12A(4659)

General description

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.

Immunogen

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

Immunogen Range: 621-670

Biochem/physiol Actions

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.

Features and Benefits

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.

Physical form

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

Disclaimer

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Myosin phosphatase-targeting subunit 1 controls chromatid segregation.
Matsumura F, et al.
The Journal of Biological Chemistry, 286(12), 10825-10833 (2011)
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)
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service