Recombinant Human GRB 14 protein (His-DHFR tag N-Terminus)
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Recombinant Human GRB 14 protein (His-DHFR tag N-Terminus) is a Human Fragment protein, in the 75 to 249 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
Growth factor receptor-bound protein 14, GRB14 adapter protein, GRB14
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
One of GRB14's main roles is negative regulation of insulin signaling. It is part of a protein complex that includes the insulin receptor where it inhibits insulin receptor kinase activity. This regulation impacts cellular glucose uptake and metabolism. GRB14 plays a critical role in controlling cell growth differentiation and survival due to its regulatory function in these pathways.
Pathways
GRB14 is involved extensively in the insulin and IGF (Insulin-like Growth Factor) receptor signaling pathways. It interacts closely with proteins such as the insulin receptor and IGF1 receptor. This interaction with receptor kinases positions GRB14 as a modulator of metabolic pathways influencing cellular energy balance and nutrient regulation.
Specifications
Form
Lyophilized
Additional notes
Purified via His tag
General info
Function
Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal.
Sequence similarities
Belongs to the GRB7/10/14 family.
Post-translational modifications
Phosphorylated on serine residues. Phosphorylated on tyrosine residues by TEK/TIE2.
Subcellular localisation
Endosome membrane
Target data
Product promise
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