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may regulate renin release and renal ion transport. Additionally we are shipping Protein Kinase, CGMP-Dependent, Type II Antibodies (54) and and many more products for this protein.
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This study indicates that loss of PRKG2 function results in differential expression of P53 (show TP53 ELISA Kits) regulated genes as well as additional pathways consistent with increased proliferation and apoptosis in the growth plate due to achondroplastic dwarfism.
PRKG2 R678X as a causative mutation for dwarfism cattle was presented.
These affinity and activation measurements show that beta-phenyl-1,N2-ethenoguanosine 3',5'-monophosphate (PET-cGMP) is most selective for PKG (show PRKG1 ELISA Kits) I, whereas 8-(4-chlorophenylthio)guanosine-3'-5'-cyclic monophosphate (8-pCPT-cGMP) is most selective for PKG (show PRKG1 ELISA Kits) II.
PKG (show PRKG1 ELISA Kits) II inhibits EGFinduced activation of HER2 (show ERBB2 ELISA Kits) through binding with and causing threonine 686 phosphorylation of this oncogenic protein.
The C-terminal cyclic nucleotide binding (CNB-B) domain of cGMP-dependent protein kinase II binds cGMP with higher affinity and selectivity when compared with its N-terminal CNB (CNB-A) domain.
Han Chinese patients with rs10033237 polymorphism of cGKII/PRKG2 gene are more likely to suffer from gout.
Our replication study suggests that cGKII is not involved in gout susceptibility.
we determined a crystal structure of the PKG (show PRKG1 ELISA Kits) II LZ-Rab11b (show RAB11B ELISA Kits) complex. The PKG (show PRKG1 ELISA Kits) II LZ domain presents a mostly nonpolar surface onto which Rab11b (show RAB11B ELISA Kits) docks, through van (show TNIP1 ELISA Kits) der (show GDF3 ELISA Kits) Waals interactions
PKGII inhibits RhoA (show RHOA ELISA Kits) activity by binding to this small GTPase (show RACGAP1 ELISA Kits) and causing phosphorylation at its Ser188 site.
PKG (show PRKG1 ELISA Kits) II also inhibits the activation of the EGFR (show EGFR ELISA Kits) caused by diverse ligands of the receptor.
These data suggest that increased PKG (show PRKG1 ELISA Kits) II activity attenuates bFGFinduced proliferation and migration by inhibiting the MAPK/ERK (show MAPK1 ELISA Kits) signaling pathway, whereas PKG (show PRKG1 ELISA Kits) I does not
type II cGMPdependent protein kinase (show CDK7 ELISA Kits) prevented the EGF (show EGF ELISA Kits)-induced phosphorylation/activation of ERK (show EPHB2 ELISA Kits) and JNK (show MAPK8 ELISA Kits), but not the phosphorylation of p38MAPK (show MAPK14 ELISA Kits) induced by EGF (show EGF ELISA Kits).
cGKII may play a role in the integration of information that conveys both anxiety-provoking stimuli as well as the spatial and environmental cues that facilitate functional memory processes and appropriate behavioral response.
urine volume was decreased significantly in cGKII-KO subjected to volume load.
Cyclic GMP kinase (show GUK1 ELISA Kits) II (cGKII) inhibits NHE3 (show SLC9A3 ELISA Kits) by altering its trafficking and phosphorylating NHE3 (show SLC9A3 ELISA Kits) at three required sites
Increased PKG2 activity alters homeostasis by suppressing proliferation and apoptosis while promoting differentiation. The PKG2-dependent mechanism was shown to involve increased DUSP10 (show DUSP10 ELISA Kits) and subsequent inhibition of JNK (show MAPK8 ELISA Kits) activity.
cGKII KO mice are significantly deficient in spatial learning while exhibiting facilitated motor coordination. Data suggest that the role of cGKII may be more robust in particular regions.
cGKII and HCN2 (show HCN2 ELISA Kits) interact and colocalize with each other
The homeobox (show PRRX1 ELISA Kits) gene Nkx family is critical for the transcriptional regulation of cGK-II during chondrogenesis.
Inhibition of cGMP-dependent protein kinase II by its own splice isoform
study provides in vivo and in vitro genetic evidence that cGKII plays a critical role in C-type natriuretic peptide (show NPPC ELISA Kits)-mediated endochondral ossification
results show that the fast phase of autophosphorylation of cGMP dependent protein kinase II has a small effect on its activity, whereas the secondary phase involving Ser126 phosphorylation may generate an active form
may regulate renin release and renal ion transport
protein kinase, cGMP-dependent, type II
, cGMP-dependant type II protein kinase
, cGMP-dependent protein kinase 2
, cGMP-dependent protein kinase 2-like
, cGK 2
, cGMP-dependent protein kinase II
, CGK 2
, cGMP dependent protein kinase type II
, protein kinase cGMP- dependent type 2
, protein kinase, cGMP- dependent, type 2
, protein kinase, cGMP- dependent, type II
, type II cGMP-dependent protein kinase