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Key Documents

M3567

Sigma-Aldrich

Anti-Myosin Iβ (Nuclear) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Anti-Myh 2, Anti-Myo1c, Anti-Myr 2

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

antigen ~120 kDa

reatividade de espécies

human, mouse, canine, rat

técnica(s)

indirect immunofluorescence: 1:50 using mouse NIH3T3 cells
microarray: suitable
western blot: 1:1,000 using extract of human HeLa cells nuclei and dog MDCK cells

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... MYO1C(4641)
mouse ... Myo1c(17913)
rat ... Myo1c(65261)

Descrição geral

Myosins belong to a superfamily of actin-based motor proteins comprising to date at least 15 classes. Myosin I (also designated myosin-1c, myo1c, M1C, myr 2 and myh 2) is a widely distributed single-headed myosin composed of an N-terminal motor domain, a calmodulin-light chain binding neck region, and a short C-terminal domain. In mammalian cells, myosin I is usually found in the cytoplasm and is especially enriched in perinuclear regions and dynamic cell margins. Myosin Iβ is found in a variety of cells such as kidney tubular cells and inner-ear hair cells.

Especificidade

Recognizes the heavy chain of the nuclear form of human myosin Iβ. Additional bands may be detected in some preparations.

Imunogênio

synthetic peptide corresponding to amino acid residues 1-16 of the heavy chain of mouse myosin Iβ (nuclear form). This sequence is missing from the other myosin I isoforms as well as from other currently known myosins.

Aplicação

Anti-Myosin Iβ (Nuclear) antibody produced in rabbit has been used in:
  • western blot
  • confocal immunofluorescence
  • immunogold labeling
  • immunofluorescence
  • co-immunoprecipitation experiments
  • immunostaining

Ações bioquímicas/fisiológicas

Myosin I is involved in cell motility, microvilli anchorage, vesicular and organelle transport and signal transduction. Myosin I associate with lipid membranes through its tail domain while its motor domain interacts with actin filaments. Myosin Iβ (nuclear) co-localizes with RNA polymerases I and II and possibly acts as a molecular motor to power transcription.

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 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

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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Specific nuclear localizing sequence directs two myosin isoforms to the cell nucleus in calmodulin-sensitive manner
Dzijak R, et al.
PLoS ONE, 7(1), e30529-e30529 (2012)
Junya Hasegawa et al.
The EMBO journal, 35(17), 1853-1867 (2016-06-25)
Autophagy is a multistep membrane traffic pathway. In contrast to autophagosome formation, the mechanisms underlying autophagosome-lysosome fusion remain largely unknown. Here, we describe a novel autophagy regulator, inositol polyphosphate-5-phosphatase E (INPP5E), involved in autophagosome-lysosome fusion process. In neuronal cells, INPP5E knockdown
Force Generation by Membrane-Associated Myosin-I
Pyrpassopoulos S, et al.
Scientific Reports (2016)
Subnuclear compartmentalization and function of actin and nuclear Myosin I in plants
Cruz JR, et al.
Chromosoma, 118(2), 193-207 (2009)
Motor domain-dependent localization of myo1b (myr-1)
Tang N, et al.
Current Biology, 11(14), 1131-1135 (2001)

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