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The product of GRB14 belongs to a small family of adapter proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. Additionally we are shipping GRB14 Antibodies (46) and GRB14 Kits (23) and many more products for this protein.
Showing 5 out of 5 products:
Study reveals that Grb14 acts as a new signaling node that regulates lipogenesis and modulates insulin sensitivity in the liver by acting at a crossroad between the insulin receptor and the p62-Nrf2-LXR signaling pathways.
The phosphorylation status of the BPS region of Grb14 determines the positive or negative role it will play in insulin receptor (show INSR Proteins) signaling.
Data show that Grb14 inhibits the activity of PTP1B (show PTPN1 Proteins) in retina in a phosphorylation-regulated (show PHAX Proteins) manner, and that rhodopsin-regulated Src kinase (show CSK Proteins) activation in retina leads to the phosphorylation of Grb14.
Grb14 is a normal physiological modulator of CNG (show CNGA1 Proteins) channel function in vivo.
Grb14 functions in vivo as a tissue-specific modulator of insulin (show INS Proteins) action, most likely via repression of IR-mediated IRS-1 (show IRS1 Proteins) tyrosine phosphorylation
regulation of Grb14 expression in adipose tissue may play a physiological role in insulin (show INS Proteins) sensitivity
Grb14 exerts a dual role on the regulation by insulin (show INS Proteins) of hepatic metabolism. It inhibits insulin receptor (show INSR Proteins) catalytic activity, and as a sterol regulatory element binding protein (show CNBP Proteins)-1c maturation.
These results demonstrate that Grb14 can undergo subcellular redistribution upon illumination and suggest that rhodopsin photoexcitation may trigger signaling events alternative to the classical transducin (show GNAT1 Proteins) activation.
Grb10 (show GRB10 Proteins) and Grb14 have roles in regulation of insulin (show INS Proteins) signaling and glucose homeostasis
The N-terminus of the BPS domain plays an important role in the regulation of human Grb14 and insulin receptor (show INSR Proteins) complex formation through phosphorylation, in addition to other domains.
Data suggest that GRB10 (show GRB10 Proteins) and GRB14 are both Ca2 (show CA2 Proteins)+-dependent CaM (show CALM1 Proteins)-binding proteins; more than one CaM (show CALM1 Proteins)-binding site and/or accessory CaM (show CALM1 Proteins)-binding sites appear to exist in GRB10 (show GRB10 Proteins) and GRB14, as compared to a single one present in GRB7 (show GRB7 Proteins). (GRB10 (show GRB10 Proteins) = growth factor receptor-bound protein 10 (show GRB10 Proteins); GRB14 = growth factor receptor-bound protein 14; CaM (show CALM1 Proteins) = calmodulin (show CALM1 Proteins); GRB7 (show GRB7 Proteins) = growth factor receptor-bound protein 7 (show GRB7 Proteins))
Colorectal cancer patients with high GRB14 levels had a shorter survival and GRB14 was upregulated at an advanced clinical stage with enhanced tumor invasion and lymph node metastasis.
Phosphorylation of Grb14 BPS domain by GSK-3 correlates with complex forming of Grb14 and insulin receptor (show INSR Proteins).
Genes within recently identified loci associated with waist-hip ratio (WHR) exhibit fat depot-specific mRNA expression, which correlates with obesity-related traits. Adipose tissue (AT) mRNA expression of 6 genes (TBX15 (show TBX15 Proteins)/WARS2 (show WARS2 Proteins), STAB1, PIGC (show PIGC Proteins), ZNRF3 (show ZNRF3 Proteins), GRB14
Modulation of mouse rod photoreceptor responses by Grb14 protein.
ANKRD55 rs459193 and GRB14 rs13389219 associate with insulin (show INS Proteins) resistance.
Studies indicate that insulin receptor (IR (show INSR Proteins)) and IGF Type 1 Receptor (IGFR) have been identified as important partners of Grb10 (show GRB10 Proteins)/14 and SH2B1 (show SH2B1 Proteins)/B2 adaptors.
Grb14 is the first negative regulator of CEACAM3 (show CEACAM3 Proteins)-initiated bacterial phagocytosis and might help to focus granulocyte responses to the subcellular sites of pathogen-host cell contact
A new role for Grb14 in finely tuning receptor signaling and modulating thyroid cancer progression.
These findings suggest that Grb14 may play a regulatory role in granulosa cells during follicular deviation in cattle.
The growth factor receptor (show RYK Proteins) bound protein (Grb) 14 NPXY motif could be acting as a dominant negative for insulin receptor (show INSR Proteins) substrate (IRS)-1 (show IRS1 Proteins) functions in the retina.
Grb14 contains a phosphorylated insulin receptor interacting domain between the pleckstrin homolog) and SH2 domains that binds to and forms a specific complex with the cytoplasmic domain of IRbeta
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 insulin receptors and insulin-like growth-factor receptors. This protein likely has an inhibitory effect on receptor tyrosine kinase signaling and, in particular, on insulin receptor signaling. This gene may play a role in signaling pathways that regulate growth and metabolism. Transcript variants have been reported for this gene, but their full-length natures have not been determined to date.
growth factor receptor-bound protein 14
, growth factor receptor-bound protein 14-like
, GRB14 adapter protein
, growth factor receptor bound protein 14