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Merck

SRP5132

Sigma-Aldrich

SMAD3, GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

别名:

DKFZP586N0721, DKFZp686J10186, HSPC193, HsT17436, JV15-2, MADH3, MGC60396

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About This Item

分類程式碼代碼:
12352200
NACRES:
NA.32

生物源

human

重組細胞

expressed in E. coli

化驗

≥70% (SDS-PAGE)

形狀

buffered aqueous glycerol solution

分子量

~77 kDa

NCBI登錄號

應用

cell analysis

運輸包裝

dry ice

儲存溫度

−70°C

基因資訊

human ... SMAD3(4088)

一般說明

SMAD3 is a direct mediator of transcriptional activation by the TGFβ receptor. The activity of SMAD3 is regulated by the TGFβ receptors, and SMAD3 is phosphorylated and associated with the ligand-bound receptor complex. TGFβ stimulation leads to phosphorylation and activation of SMAD3, which form a complex with SMAD4 that accumulate in the nucleus and regulate transcription of target genes such as CDK inhibitor. SMAD3 containing a C-terminal truncation acts as a dominant-negative inhibitor of the normal TGFβ response. SMAD3 is a major physiologic substrate of the G1 cyclin-dependent kinases CDK4 and CDK2.

外觀

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

準備報告

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Gareth J Inman et al.
Molecular cell, 10(2), 283-294 (2002-08-23)
Transforming growth factor (TGF)-beta stimulation leads to phosphorylation and activation of Smad2 and Smad3, which form complexes with Smad4 that accumulate in the nucleus and regulate transcription of target genes. Here we demonstrate that, following TGF-beta stimulation of epithelial cells
Isao Matsuura et al.
Nature, 430(6996), 226-231 (2004-07-09)
Transforming growth factor-beta (TGF-beta) potently inhibits cell cycle progression at the G1 phase. Smad3 has a key function in mediating the TGF-beta growth-inhibitory response. Here we show that Smad3 is a major physiological substrate of the G1 cyclin-dependent kinases CDK4

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