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SAB4504208

Sigma-Aldrich

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

affinity isolated antibody

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 48 kDa

Espèces réactives

rat, mouse, human

Concentration

~1 mg/mL

Technique(s)

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

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

phosphorylation (pThr8)

Informations sur le gène

Description générale

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.

Immunogène

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

Immunogen Range: 1-50

Application

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

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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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