SRP5131
SMAD2, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
别名:
JV18, JV18-1, MADH2, MADR2, MGC22139, MGC34440, hMAD-2, hSMAD2
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关于此项目
Form:
buffered aqueous glycerol solution
Assay:
≥70% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
~90 kDa
产品名称
SMAD2, GST tagged human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
biological source
human
recombinant
expressed in E. coli
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~90 kDa
NCBI accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... SMAD2(4087)
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
存储类别
10 - Combustible liquids
wgk
WGK 1
法规信息
新产品
此项目有
Alterations in the Smad pathway in human cancers.
Samanta D and Datta PK
Frontiers in Bioscience (Landmark Edition) (2012)
Signaling of transforming growth factor-beta family members through Smad proteins.
Itoh S
European Journal of Biochemistry (2000)
Targeting the transforming growth factor-beta signaling pathway in human cancer.
Nagaraj NS
Expert Opinion on Investigational Drugs (2010)
M Funaba et al.
Molecular endocrinology (Baltimore, Md.), 14(10), 1583-1591 (2000-10-24)
Smads mediate activin, transforming growth factor beta (TGFbeta), and bone morphogenetic protein signaling from receptors to nuclei. According to the current model, activated activin/TGFbeta receptors phosphorylate the carboxyl-terminal serines of Smad2 and Smad3 (SSMS-COOH); phosphorylated Smad2/3 oligomerizes with Smad4, translocates
Alison E John et al.
Methods in molecular biology (Clifton, N.J.), 1627, 351-365 (2017-08-25)
The potent and pluripotent cytokine TGFβ has important roles in normal homeostasis and disease pathogenesis. Once released from cells, TGFβ exists in both latent and functionally active forms. Large amounts of latent TGFβ are secreted from cells and sequestered in
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