Anti-cGKI/PRKG1 Antibody Picoband® Fluoro647 Conjugated

CGMP-dependent protein kinase 1, alpha isozyme is an enzyme that in humans is encoded by the PRKG1 gene. 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.

E3 SUMO-protein ligase PIAS1; DEAD/H box-binding protein 1; E3 SUMO-protein transferase PIAS1; Gu-binding protein; GBP; Protein inhibitor of activated STAT protein 1; RNA helicase II-binding protein; PIAS1; DDXBP1

Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB.

1. Burgoyne, J. R., Madhani, M., Cuello, F., Charles, R. L., Brennan, J. P., Schroder, E., Browning, D. D., Eaton, P. Cysteine redox sensor in PKGI-alpha enables oxidant-induced activation. Science 317: 1393-1397, 2007. 2. Foller, M., Feil, S., Ghoreschi, K., Koka, S., Gerling, A., Thunemann, M., Hofmann, F., Schuler, B., Vogel, J., Pichler, B., Kasinathan, R. S., Nicolay, J. P., Huber, S. M., Lang, F., Feil, R. Anemia and splenomegaly in cGKI-deficient mice. Proc. Nat. Acad. Sci. 105: 6771-6776, 2008. 3. Guo, D., Regalado, E., Casteel, D. E., Santos-Cortez, R. L., Gong, L., Kim, J. J., Dyack, S., Horne, S. G., Chang, G., Jondeau, G., Boileau, C., Coselli, J. S., and 10 others. Recurrent gain-of-function mutation in PRKG1 causes thoracic aortic aneurysms and acute aortic dissections. Am. J. Hum. Genet. 93: 398-404, 2013.