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Variation in RGS17 was associated with risk for substance dependence diagnoses in both African American and European American populations.
Two single nucleotide polymorphisms in the regulator of G-protein signaling 17 gene are associated with smoking initiation.
RGS17 is differentially expressed in hepatocellular carcinoma cells and plays a central role in regulating transformed hepatocyte tumorgenicity.
Results establish RGS10 (show RGS10 ELISA Kits) and RGS17 as novel regulators of cell survival and chemoresistance in ovarian cancer cells and suggest that their reduced expression may be diagnostic of chemoresistance.
Taken together, these data have provided the first evidence of miRNA regulation of RGS17 expression in lung cancer.
RGS17 is a new RZ member that preferentially inhibits receptor signaling via G(i/o), G(z), and G(q) over G(s) to enhance cAMP-dependent signaling and inhibit calcium signaling
RGS17, an overexpressed gene in human lung and prostate cancer, induces tumor cell proliferation through the cyclic AMP (show APRT ELISA Kits)-PKA-CREB (show CREB1 ELISA Kits) pathway.
RGS17 is a major candidate for the familial lung cancer susceptibility locus on chromosome 6q23-25.
SUMO-SIM (show STIM1 ELISA Kits) interactions regulate the activity of RGSZ2 proteins
This RGSZ2-dependent regulation of NMDAR (show GRIN1 ELISA Kits) activity is relevant to persistent pain disorders associated with heightened NMDAR (show GRIN1 ELISA Kits)-mediated glutamate (show GRIN1 ELISA Kits) responses and the reduced antinociceptive capacity of opioids.
These results indicate that the NMDAR (show GRIN1 ELISA Kits)/nNOS (show NOS1 ELISA Kits) cascade, activated via MORs, provide the free zinc ions required for inactive PKCgamma (show PRKCG ELISA Kits) to bind to HINT1 (show HINT1 ELISA Kits)/RGSZ complex at the C terminus of the receptor.
This gene encodes a member of the regulator of G-protein signaling family. This protein contains a conserved, 120 amino acid motif called the RGS domain and a cysteine-rich region. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal.
regulator of G-protein signalling 17
, regulator of G-protein signaling 17
, regulator of G-protein signaling Z2
, regulator of Gz-selective protein signaling 2
, RGS protein RGS-17