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Key Documents

SAB4504208

Sigma-Aldrich

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

affinity isolated antibody

Synonim(y):

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

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About This Item

Kod UNSPSC:
12352203
NACRES:
NA.41

pochodzenie biologiczne

rabbit

białko sprzężone

unconjugated

forma przeciwciała

affinity isolated antibody

rodzaj przeciwciała

primary antibodies

klon

polyclonal

Postać

buffered aqueous solution

masa cząsteczkowa

antigen 48 kDa

reaktywność gatunkowa

rat, mouse, human

stężenie

~1 mg/mL

metody

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

numer dostępu NCBI

numer dostępu UniProt

Warunki transportu

wet ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

phosphorylation (pThr8)

informacje o genach

Opis ogólny

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.

Immunogen

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

Immunogen Range: 1-50

Zastosowanie

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

Działania biochem./fizjol.

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.

Cechy i korzyści

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.

Postać fizyczna

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

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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