Cyclic Guanosine Monophosphate (cGMP) ELISA Kit for Human

Mammals have three different isoforms of cyclic GMP-dependent protein kinase (Ialpha, Ibeta, and II). These PRKG isoforms act as key mediators of the nitric oxide/cGMP signaling pathway and are important components of many signal transduction processes in diverse cell types. This PRKG1 gene on human chromosome 10 encodes the soluble Ialpha and Ibeta isoforms of PRKG by alternative transcript splicing. A separate gene on human chromosome 4, PRKG2, encodes the membrane-bound PRKG isoform II. The PRKG1 proteins play a central role in regulating cardiovascular and neuronal functions in addition to relaxing smooth muscle tone, preventing platelet aggregation, and modulating cell growth. This gene is most strongly expressed in all types of smooth muscle, platelets, cerebellar Purkinje cells, hippocampal neurons, and the lateral amygdala. Isoforms Ialpha and Ibeta have identical cGMP-binding and catalytic domains but differ in their leucine/isoleucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity. [provided by RefSeq, Sep 2011]

PKG1: an AGC kinase of the PKG family. Type I cGMP-dependent protein kinase; relaxes vascular smooth muscle and inhibits platelet aggregation. Binding of cGMP results in enzyme activation. Two splice variant isoforms have been described.

Protein type: EC 2.7.11.12; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor); Kinase, protein; AGC group; PKG family

Chromosomal Location of Human Ortholog: 10q11.2

Cellular Component: Golgi apparatus; cytoplasm; plasma membrane; cytosol

Molecular Function: protein binding; calcium channel regulator activity; cGMP-dependent protein kinase activity; cGMP binding; ATP binding

Biological Process: regulation of GTPase activity; relaxation of vascular smooth muscle; cGMP-mediated signaling; forebrain development; dendrite development; neuron migration; actin cytoskeleton organization and biogenesis; blood coagulation; signal transduction; protein amino acid phosphorylation