PRKG1 (protein kinase, cGMP-dependent, type I) gene is localized to human chromosome 10 and encodes the soluble Ia and Iß isoforms of PRKG by alternative transcript splicing. It contains 19 exons spanning a length of 220kb. These isoforms have identical cGMP-binding and catalytic domains but different leucine/isoleucine zipper and autoinhibitory sequences. They vary in their dimerization substrates and kinase enzyme activity.
Synonyms: Anti-CGK 1 alpha antibody produced in rabbit; Anti-cGKI-alpha antibody produced in rabbit; Anti-cGMP-dependent protein kinase 1, alpha-isozyme antibody produced in rabbit
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: PRKG1 (protein kinase, cGMP-dependent, type I) is a cyclic GMP-dependent protein kinase that functions in the relaxation of vascular smooth muscle by lowering the intracellular level of calcium. It is activated by an intracellular increase in cGMP mediated by natriuretic peptides. The activated PRKG1 phosphorylates perilipin 1 and hormone-sensitive lipase, which in turn initiate lipolysis and increase the oxidative capacity of human skeletal muscle. A gain-of-function mutation in this gene leads to a constitutively active Prkg1 even in the absence of cGMP. High levels of this protein causes decreased phosphorylation of the myosin regulatory light chain in fibroblasts and decreased contraction of vascular smooth muscle cells. This results in thoracic aortic aneurysms.
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