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M9818

Sigma-Aldrich

Anti-Myopodin antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41
conjugado:
unconjugated
application:
IHC (f)
WB
clone:
polyclonal
reatividade de espécies:
rat
citations:
5
técnica(s):
immunohistochemistry (frozen sections): 1-2 μg/mL using rat skeletal muscle and rat kidney
western blot: 1-2 μg/mL using cytosolic fraction of rat skeletal muscle

fonte biológica

rabbit

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

peso molecular

antigen 80 kDa

reatividade de espécies

rat

técnica(s)

immunohistochemistry (frozen sections): 1-2 μg/mL using rat skeletal muscle and rat kidney
western blot: 1-2 μg/mL using cytosolic fraction of rat skeletal muscle

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

Descrição geral

Myopodin (80-95 kDa), a novel actin bundling protein, is an additional member of the synaptopodin gene family. Myopodin is expressed in skeletal and cardiac muscles. Myopodin contains one PPXY motif, multiple PXXP motifs, and a nuclear export sequence (NES). In the-disc, myopodin colocalizes with α-actinin. Myopodin, like several actin-bundling proteins, has been shown to shuttle between the nucleus and cytoplasm. It is localized in nucleus in myoblasts.

Imunogênio

synthetic peptide encoding amino acids 566-585 located at the mid-region of human myopodin, conjugated to KLH. This sequence is highly conserved (77% sequence identity) in mouse myopodin and is not found in human or rat synaptopodin.

Aplicação

Anti-Myopodin has been used in:
  • immunohistochemistry
  • immunostaining
  • western blot analysis

Ações bioquímicas/fisiológicas

Myopodin directly binds to actin and contains an actin-binding site in the centre of the protein. Myopodin has actin bundling activity as shown by lantraculin - a sensitive cytosolic actin bundles and nuclear actin loops in transfected cells expressing GFP-myopodin. It binds to stress fibres in a punctuated pattern into the Z-disc during myotube differentiation. Myopodin is frequently down-regulated in invasive stages of some types of cancers, including invasive bladder tumors. Frequent complete or partial deletions of the myopodin gene have been shown to occur in 80% of invasive prostate cancer cases. Expression of myopodin induces suppression of tumor growth both in vivo and in vitro. Myopodin inhibits tumor metastasis by functioning as a tumor suppressor gene.

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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)

nwg

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Visite a Biblioteca de Documentos

Tumor suppressor role for myopodin in bladder cancer: loss of nuclear expression of myopodin is cell-cycle dependent and predicts clinical outcome
Sanchez-Carbayo M, et al.
Oncogene, 22(34), 5298-5298 (2003)
Interaction between importin 13 and myopodin suggests a nuclear import pathway for myopodin
Liang J, et al.
Molecular and Cellular Biochemistry, 307(1-2), 93-100 (2008)
Myopodin, a synaptopodin homologue, is frequently deleted in invasive prostate cancers
Lin F, et al.
The American Journal of Pathology, 159(5), 1603-1612 (2001)
Expression of myopodin induces suppression of tumor growth and metastasis
Jing L, et al.
The American Journal of Pathology, 164(5), 1799-1806 (2004)
Differentiation-and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein
Weins A, et al.
The Journal of Cell Biology, 155(3), 393-404 (2001)

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