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SAB4504208

Sigma-Aldrich

Anti-phospho-Smad2/3 (pThr8) antibody produced in rabbit

affinity isolated antibody

Sinônimo(s):

Anti-HSPC193, Anti-HsT17436, Anti-JV15-2, Anti-LDS1C, Anti-LDS3, Anti-MADH3

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About This Item

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

Formulário

buffered aqueous solution

peso molecular

antigen 48 kDa

reatividade de espécies

rat, mouse, human

concentração

~1 mg/mL

técnica(s)

ELISA: 1:10000
western blot: 1:500-1:1000

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

phosphorylation (pThr8)

Informações sobre genes

Descrição geral

SMAD3 (homologues of the Drosophila protein, mothers against decapentaplegic (Mad) and the Caenorhabditis elegans protein) is located on human chromosome 15q22. SMAD2 (SMAD family member 2) is also called as MADR2 (substrate of the TGFβ receptor). It is located on human chromosome 18q21. Smad2/3 belongs to the mothers against Dpp (MAD) related family of proteins. SMAD2 has two highly conserved amino and carboxyl-terminal domains (MH1 and MH2 domains) but has no known structural motifs.

Imunogênio

The antiserum was produced against synthesized peptide derived from human Smad2/3 around the phosphorylation site of Thr8.

Immunogen Range: 1-50

Aplicação

Anti-phospho-Smad3 (pSer425) antibody has been used in western blotting.

Ações bioquímicas/fisiológicas

SMAD (homologues of the Drosophila protein, mothers against decapentaplegic (Mad) and the Caenorhabditis elegans protein) proteins play an important role in the intracellular signalling of transforming growth factor β (TGFβ). Reduction in the phosphorylation level of Smad3 helps autophagy to control the endothelial-mesenchymal transition. In human arterial smooth muscle cells, suppressing siRNA of SMAD3 improves the viability of cells. Mutations in SMAD2 (SMAD family member 2) results in arterial aneurysms and dissections. Upregulation of Smad2 blocks the multiplication of gingival epithelial cells. It plays an important role in TGF-β (transforming growth factor β)/activin signaling pathways. Smad2 positively and negatively controls TGFβ-dependent transcription with the help of forkhead DNA-binding protein FAST2.

Características e benefícios

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.

forma física

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

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 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Absence of chloride intracellular channel 4 (CLIC4) predisposes to acute kidney injury but has minimal impact on recovery
Edwards JC, et al.
BMC Nephrology (2014)
Effects of FSTL1 on cell proliferation in breast cancer cell line MDA?MB?231 and its brain metastatic variant MDA?MB?231?BR
An J, et al.
Oncology Reports, 38(5), 3001-3010 (2017)
Smad2 and Smad3 Positively and Negatively Regulate TGF?-Dependent Transcription through the Forkhead DNA-Binding Protein FAST2
Labbe E, et al.
Molecular Cell (1998)
Frequency of Smad Gene Mutations in Human Cancers'
Riggins G J, et al.
Cancer Research (1997)
Jiaqiang An et al.
Oncology reports, 38(5), 3001-3010 (2017-10-20)
In the past decades, altered Follistatin‑like 1 (FSTL1) expression has been documented in a variety of cancers, while its functional roles are poorly understood. Particularly in breast cancer, the expression of FSTL1 and its signaling pathway remain to be determined. In the

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