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Merck

M9818

Sigma-Aldrich

Anti-Myopodin antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL番号:
UNSPSCコード:
12352203
NACRES:
NA.41
結合体:
unconjugated
application:
IHC (f)
WB
クローン:
polyclonal
化学種の反応性:
rat
citations:
5
テクニック:
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

由来生物

rabbit

品質水準

結合体

unconjugated

抗体製品の状態

affinity isolated antibody

抗体製品タイプ

primary antibodies

クローン

polyclonal

フォーム

buffered aqueous solution

分子量

antigen 80 kDa

化学種の反応性

rat

テクニック

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

UniProtアクセッション番号

輸送温度

dry ice

保管温度

−20°C

ターゲットの翻訳後修飾

unmodified

遺伝子情報

詳細

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.

免疫原

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.

アプリケーション

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

生物化学的/生理学的作用

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.

物理的形状

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

免責事項

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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保管分類コード

10 - Combustible liquids

WGK

nwg

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

IXO11497:
M9818-200UL:
M9818-VAR:
M9818-BULK:


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Lot/Batch Number

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文書ライブラリにアクセスする

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)
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)
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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