M8064

Anti-Myosin IIA, non muscle antibody produced in rabbit

Name: Anti-Myosin IIA, non muscle antibody produced in rabbit
Brand: SIGMA

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-BDPLT6, Anti-DFNA17, Anti-EPSTS, Anti-FTNS, Anti-MATINS, Anti-MHA, Anti-NMHC-II-A, Anti-NMMHC-IIA, Anti-NMMHCA

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About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

MDL number:

MFCD03455610

Nom du produit

Anti-Myosin IIA, non muscle antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~200 kDa

species reactivity

rat, human, canine

packaging

antibody small pack of 25 μL

technique(s)

indirect immunofluorescence: 1:100 using cultured rat NRK cells
microarray: suitable
western blot: 1:1,000 using whole cell extracts of cultured dog MDCK kidney cells and cultured human Jurkat cells

UniProt accession no.

P35579

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

Gene Information

human ... MYH9(4627)
rat ... Myh9(25745)

Application

Anti-Myosin IIA, non muscle antibody produced in rabbit has been used in:

immunofluorescence
immunohistochemistry
fixed cell staining/ immunofluorescence staining
immunoblot
immunoprecipitation

Biochem/physiol Actions

Nonmuscle myosin II is involved in cell motility and adhesion, cytokinesis, vesicular transport, intracellular force generation and in morphogenesis during development. Its activity is regulated by light chain and possibly heavy chain phosphorylation and by association with proteins such as Mts1. Mutations in the NMHCA gene are found in several syndromes associated with megakaryocyte/platelet/leukocyte disorders. Mutations in the MYH9 gene causes a spectrum of macrothrombocytopenia disorders with neutrophil inclusions, termed as MYH9 disorders.

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.

General description

Myosin heavy chain 9 (MYH9) gene codes for the nonmuscle myosin heavy chain IIA.

Myosin heavy chain 9 is expressed in platelets and the gene encoding it is localized on chromosome 22.

Immunogen

synthetic peptide corresponding to amino acids 1949-1960 of human nonmuscle myosin IIA.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.

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Classe de stockage

12 - Non Combustible Liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

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Consulter la Bibliothèque de documents

The role of stress fibers in the shape determination mechanism of fish keratocytes

Nakata T, et al.

Biophysical Journal, 110(2), 481-492 (2016)

Nonmuscle myosin-2: mix and match

Heissler SM and Manstein DJ

Cellular and Molecular Life Sciences, 70(1), 1-21 (2013)

The abnormal proplatelet formation in MYH9-related macrothrombocytopenia results from an increased actomyosin contractility and is rescued by myosin IIA inhibition.

Y Chen et al.

Journal of thrombosis and haemostasis : JTH, 11(12), 2163-2175 (2013-10-30)

Mutations in the MYH9 gene cause autosomal dominant MYH9-related diseases (MYH9-RD) that associate macrothrombocytopenia with various other clinical conditions. The mechanisms giving rise to giant platelets remain poorly understood. To study the proplatelet formation (PPF) derived from megakaryocytes (MKs) generated

Adhesion-dependent and contractile ring-independent equatorial furrowing during cytokinesis in mammalian cells

Kanada M, et al.

Molecular Biology of the Cell, 16(8), 3865-3872 (2005)

A mechanism of leading-edge protrusion in the absence of Arp2/3 complex.

Praveen Suraneni et al.

Molecular biology of the cell, 26(5), 901-912 (2015-01-09)

Cells employ protrusive leading edges to navigate and promote their migration in diverse physiological environments. Classical models of leading-edge protrusion rely on a treadmilling dendritic actin network that undergoes continuous assembly nucleated by the Arp2/3 complex, forming ruffling lamellipodia. Recent

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Data Sheet - M8064

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