Particulate Gunylate Cyclase C (PGCC) from MyBioSource.com

Alternate nomenclature: Sta-R Cyclic GMP (cGMP), a key messenger in several signal transduction pathways, the intracellular levels of cGMP are maintained by the activity of opposing enzymes: synthesizing gualylyl cyclases (GC) and hydrolyzing phosphodiesterases (PDEs). The synthesizing enzymes (GCs) are found in two forms: cytosolic (soluble) and membrane-bound (particulate), while they share similar structural characteristics, they differ in their mechanisms of physiological regulations. Most importantly, soluble GC (sGC) contains a heme group and binds NO that activates the enzyme, while particulate GC (PGCs) are stimulated by natriuretic peptides. Particulate forms of guanylyl cyclases have been shown to function as natriuretic peptide receptors. In response to G-protein coupled receptor stimulation, the cGMP can be produced from GTP by either soluble guanylate cyclase (sGC), or by PGC. The sGC are heterodimers (alpha & beta polypeptide chains), that are stimulated by nitric oxide and carbon monoxide or by particulate membrane-bound guanylyl cyclases which are activated by a complex mechanism by natriuretic peptides. PGCs have 7 different isoforms, PGC-A through PGC-G and are expressed in most tissues in isoform specific manner (See Table 1). There is significant structural homology among various PGCs, there is a large N-terminal extracellular domain (ECD), a single TMD and a large intracellular domain with protein kinase activity (KLD), a C-terminal catalytic domain (CD) and in between is a dimmerization domain (DD). Guanylyl cyclase C (PGC-C), a member of membrane-bound guanylyl cyclases, is a receptor protein for guanylin and uroguanylin. The binding of a ligand to the extracellular domain of PGC-C triggers signal transduction, resulting in the regulation of intestinal fluids and electrolytes (2). A previous study proposed that a ligand-binding site on PGC-C is localized near the trans-membrane region. The PGC-C type guanylate cyclase is a receptor for heat stable enterotoxin. PGC-c protein contains an extracellular amino acid sequence that is divergent from other PGCs, but retains several structural motifs (KLD, ECD and TMD). Disrupted activity of PGC-C may be involved in acute diarrhea. The Anti-PGC-C-selective antibodies were generated against conserved sequences near the C-terminal end of the protein that are unique to PGC-C protein. The PGC-C-selective antibodies are affinity purified against immobilized antigen based affinity chromatography that yielded epitope-specific antibodies. The PGC-C antibodies label a 127-130 kDa protein in various tissues including intestine, kidney and spleen. Anti- PGC-C-selective antibodies are also available in affinity-purified form for confocal, WB, IHC analyses. MyBioSource will also conjugate antibodies with fluorescent probes upon request at extra charge. MyBioSource also provides antibodies to other family members of the particulate GC (PGA, B, D, E, F and G) and to various adenylate cyclases (AC-1 through 9). MyBioSource employs cyclic peptide methodology for generating antibodies, which results in higher titer and specificity (6). MyBioSource, will also provide Western blot positive controls for most of these antibodies in ready-to-use buffer for easy identification of respective proteins. Limited quantities of antigens are also available for blocking studies. Please enquire for their availability before ordering