SRP5134
SMAD5, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
DKFZp781C1895, DKFZp781O1323, Dwfc, JV5-1, MADH5
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
recombinant
expressed in E. coli
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~82 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... SMAD5(4090)
General description
SMAD5 is a member of the SMAD family and mediates signaling by the transforming growth factor-beta (TGFβ) superfamily and related ligands. SMAD5 plays a critical role in the signaling pathway by which TGFβ inhibits the proliferation of human hematopoietic progenitor cells. SMAD5 is up-regulated in gastric epithelial cells during the infection of the pathogen Helicobacter pylori and it mediates apoptosis of gastric epithelial cells induced by H. pylori infection. In mature human B cells, bone morphogenetic protein 6 (BMP-6) inhibits cell growth and rapidly induces phosphorylation of SMADs 5 and 8.
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
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
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Tomokazu Nagasako et al.
The Journal of biological chemistry, 278(7), 4821-4825 (2002-12-11)
The gastric pathogen Helicobacter pylori activates epithelial cell signaling pathways, and its infection induces changes in the expression of several genes in infected human gastric tissues. Recent studies have indicated that the ability of H. pylori to regulate epithelial cell
C H Heldin et al.
Nature, 390(6659), 465-471 (1997-12-11)
The recent identification of the SMAD family of signal transducer proteins has unravelled the mechanisms by which transforming growth factor-beta (TGF-beta) signals from the cell membrane to the nucleus. Pathway-restricted SMADs are phosphorylated by specific cell-surface receptors that have serine/threonine
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