SRP5184
GRB2, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
ASH, EGFRBP-GRB2, Grb3-3, MST084, MSTP084
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About This Item
biological source
human
recombinant
expressed in E. coli
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~49 kDa
NCBI accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... GRB2(2885)
General description
GRB2 is an adaptor protein that is the homolog of the Sem5 gene of C. elegans and Drk gene of Drosophila. GRB2 protein contains one SH2 domain and two SH3 domains and plays a role in growth factor-mediated signal transduction. GRB2 forms a complex with activated EGFR and the RAS-specific guanine nucleotide exchange factor SOS1 thereby mediating the growth factor-induced activation of RAS. GRB2 has been implicated in growth factor regulation of the cytoskeleton and DNA synthesis. DAB2 also binds to GRB2 and competes with SOS for GRB2 binding. GRB2 interacts with the hepatitis C virus nonstructural 5A (NS5A) protein and inhibits the activation of ERK1 and ERK2 by EGF.
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
flash_point_f
Not applicable
flash_point_c
Not applicable
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S L Tan et al.
Proceedings of the National Academy of Sciences of the United States of America, 96(10), 5533-5538 (1999-05-13)
Although hepatitis C virus (HCV) infection is an emerging global epidemic causing severe liver disorders, the molecular mechanisms of HCV pathogenesis remain elusive. The NS5A nonstructural protein of HCV contains several proline-rich sequences consistent with Src homology (SH) 3-binding sites
E J Lowenstein et al.
Cell, 70(3), 431-442 (1992-08-07)
A cDNA clone encoding a novel, widely expressed protein (called growth factor receptor-bound protein 2 or GRB2) containing one src homology 2 (SH2) domain and two SH3 domains was isolated. Immunoblotting experiments indicate that GRB2 associates with tyrosine-phosphorylated epidermal growth
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