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anti-Mouse (Murine) GRB7 Antibodies:
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Human Polyclonal GRB7 Primary Antibody for EIA, WB - ABIN952626
Depetris, Wu, Hubbard: Structural and functional studies of the Ras-associating and pleckstrin-homology domains of Grb10 and Grb14. in Nature structural & molecular biology 2009
Show all 5 references for ABIN952626
Human Polyclonal GRB7 Primary Antibody for WB - ABIN374205
Margolis, Silvennoinen, Comoglio, Roonprapunt, Skolnik, Ullrich, Schlessinger: High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains. in Proceedings of the National Academy of Sciences of the United States of America 1992
Show all 2 references for ABIN374205
GRB7 gene expression in uterus during embryo implantation is regulated by Mmu-miR (show MLXIP Antibodies)-193.
Findings illustrate an underlying mechanism by which Grb7 promotes tumorigenesis through the formation of a novel EGFR (show EGFR Antibodies)-Grb7-Ras signaling complex, thereby highlighting the potential strategy of targeting Grb7 as an anti-breast cancer therapy.
The adaptor Grb7 links netrin-1 (show NTN1 Antibodies) signaling to regulation of mRNA translation of kappa opioid receptor (show OPRK1 Antibodies).
Grb7 is identified as an integral component of stress granules.
Suggest close relationship between Grb7 gene amplification and GRB7 protein overexpression in human ovarian cancer. Immunohistochemistry might have limited diagnostic value in these tumors compared to fluorescence in situ hybridization.
Grb7 was found to be significantly related to the biological classification of breast cancer
apo (show C9orf3 Antibodies) Grb7 SH2 domain crystallized in the trigonal space group P63 (show RPE65 Antibodies), whereas the G7-B1-Grb7 SH2 domain complex crystallized in the monoclinic space group P21 (show CDKN1A Antibodies)
The data reveal that Grb7 plays an important role in breast cancer progression, beyond the context of HER2 (show ERBB2 Antibodies)+ve cell types
Grb7 protein interacts with Filamin-a, an actin-crosslinking component of the cell cytoskeleton.
Data suggest that calmodulin (show CALM1 Antibodies) controls Grb7-mediated cell migration.
Data propose the phosphorylation state of Grb7-SH2 domain tyrosine residues could control Grb7 dimerization, and dimerization may be an important regulatory step in Grb7 binding to RTKs such as erbB2 (show ERBB2 Antibodies).
GRB7 is a context-dependent oncogene (show RAB1A Antibodies), which modulates the ERBB2 (show ERBB2 Antibodies) signaling pathway through enhanced phosphorylation of ERBB2 (show ERBB2 Antibodies) and Akt (show AKT1 Antibodies).
propose that CaM (show CALM1 Antibodies) inhibits the translocation of Grb7 to the nucleus after binding to its CaM (show CALM1 Antibodies)-BD and therefore occluding its overlapping NLS (show ALDH1A2 Antibodies)
A series of Grb7 SH2 domain-binding nonphosphorylated peptides in the yeast two-hybrid system, were identified.
The product of this gene belongs to a small family of adapter proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. This gene encodes a growth factor receptor-binding protein that interacts with epidermal growth factor receptor (EGFR) and ephrin receptors. The protein plays a role in the integrin signaling pathway and cell migration by binding with focal adhesion kinase (FAK). Several transcript variants encoding two different isoforms have been found for this gene.
growth factor receptor-bound protein 7
, growth factor receptor-bound protein 7-like
, GRB7 adapter protein
, Growth factor receptor-bound protein 7 (GRB7 adapter protein) (Epidermal growth factor receptor GRB-7)
, epidermal growth factor receptor GRB-7
, growth factor receptor binding protein GRB7