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Human Red Blood Cells carry catalytically active alpha1beta1-soluble guanylate cyclase (isoform 1). Red cell soluble guanylate cyclase activity is fully preserved in patients with stable coronary artery disease.
Inhibition of HDAC3 (show HDAC3 Proteins) with targeted therapy could benefit treatment of the diseases associated with sGCbeta1 down-regulation and/or deficiency such as cancer and several vascular-related diseases.
The kinetics of heme loss from oxidized sGC (show SGCB Proteins) was monitored by a new method based on the heme group de-quenching the fluorescence of FlAsH-EDT2.
Dynamic interplay between hsp90 (show HSP90 Proteins), apo (show C9orf3 Proteins)-sGC (show SGCB Proteins)-beta1, and sGC (show SGCB Proteins)-alpha1 in response to NO is unprecedented and represent new steps by which cells can modulate the heme content and activity of sGC (show SGCB Proteins) for signaling cascades.
Gene expression in dendritic cells of CCL5 (show CCL5 Proteins) and CXCL5 (show CXCL5 Proteins) as well as TIMP1 (show TIMP1 Proteins) and GUCY1B3 showed a significant increase within the first 4 days after trauma.
The G-protein regulator LGN modulates the activity of the NO receptor soluble guanylate cyclase
We concluded that the alpha-subunit (show POLG Proteins) and the beta(1)(191-619) domain exert structural strains on the heme domain.
Data show that show that it is possible to directly monitor the sGC (show SGCB Proteins) haem oxidation state in intact cells. By inserting the TC motif into the coding sequence of the beta1 subunit of sGC (show SGCB Proteins) in transiently transfected Chinese hamster ovary cells.
recombinant soluble guanylate cyclase (sGC (show SGCB Proteins)) beta1 subunit and truncated N-terminal fragments expressed in E. coli; studied interaction between NO and sGC (show SGCB Proteins) and schematic mechanism was proposed; study provides insights into structure and NO-binding of sGC (show SGCB Proteins)
Results show that NOGCbeta1 and GC-A (show NPR1 Proteins) interact and that NOGCbeta1 regulates atrial natriuretic peptide (show NPPA Proteins) signaling in HK-2 (show HK2 Proteins) cells.
expression of sGC (show NPR1 Proteins) beta(1)-subunit in pulmonary arteries increased with postnatal age both at the level of mRNA and protein
These results suggest a means by which the hsp90beta (show HSP90AB1 Proteins) interaction could prevent apo (show C9orf3 Proteins)-sGCbeta1 from associating with its partner sGCalpha1 subunit while enabling structural changes to assist heme insertion into the H-NOX domain.
Study shows notch (show NOTCH1 Proteins) signaling provides a constitutive drive on expression of the major nitric oxide receptor GUCY1A3 (show GUCY1A3 Proteins) and GUCY1B3 in arteries from mice.
Apo (show C9orf3 Proteins)-sGC (show NPR1 Proteins) mice expressing haem-free sGC (show NPR1 Proteins) are viable and develop hypertension. The haemodynamic effects of NO are abolished, but those of the sGC (show NPR1 Proteins) activator cinaciguat are enhanced.
sGC (show NPR1 Proteins) and cGMP-dependent signaling are necessary and sufficient for HNO-induced vasodilation in vivo but are not required for positive inotropic action.
Deletion of GCbeta1 specifically in smooth muscle cells abolishes NO-induced corpus cavernosum relaxation but does not lead to infertility.
A VASP (show VASP Proteins) to Rac (show AKT1 Proteins) to soluble guanylyl cyclase negative feedback loop limited cGMP production, thereby regulating adipogenesis and energy homeostasis.
These data suggests a novel physiological role for PDE5 (show PDE5A Proteins) in restricting the effects of NOS3 (show NOS3 Proteins)/sGC (show NPR1 Proteins)/PKG (show PRKG1 Proteins) signaling pathway to modulating beta-AR stimulated I(Ca), while limiting effects on cardiac contraction.[sGC (show NPR1 Proteins)]
Pressure overload results in translocation of sGC (show NPR1 Proteins) out of membrane microdomains, depressing NO/heme-dependent activation in the heart, consistent with enhanced oxidation.
Important roles of sGC (show NPR1 Proteins) in stimulating platelet activation and in vivo thrombosis and hemostasis.
findings identify a crucial role of the NO/sGCalpha1beta1/cGMP pathway in modulating lymphatic vessel function [soluble guanylate cyclase alpha1beta1]
Knockout of GCbeta1 completely disrupts the NO/cGMP signaling cascade and provides evidence for the unique role of NO-GC as NO receptor.
Soluble guanylate cyclase (sGC), a heterodimeric protein consisting of an alpha subunit and a beta subunit, typically GUCY1B3, catalyzes conversion of GTP to the second messenger cGMP and functions as the main receptor for nitric oxide (NO) and nitrovasodilator drugs (Zabel et al., 1998
guanylate cyclase 1, soluble, beta 3
, guanylate cyclase soluble subunit beta-1-like
, guanylate cyclase soluble subunit beta-1
, soluble guanylyl cyclase beta subunit
, guanylate cyclase soluble subunit beta-3
, soluble guanylate cyclase small subunit
, soluble guanylate cyclase 1 beta 3
, soluble guanylyl cyclase beta 1 subunit
, NO-sensitive GC beta 1 subunit
, nitric oxide-sensitive guanylyl cyclase beta 1 subunit
, NO-sensitive guanylyl cyclase beta 1 subunit
, beta 1 sGC
, soluble guanylate cyclase beta-1 subunit
, guanylate cyclase, soluble, beta 1