Guanylate cyclases belong to the adenylyl cyclase class-4/guanylyl cyclase family. There are two forms of guanylate cyclase, a soluble form (GCS or sGC), which act as receptors for nitric oxide and a membrane-bound receptor form (GC), which are peptide hormone receptors. The GC-C protein is composed of an extracellular domain, a single transmembrane domain, and a cytoplasmic region consisting of a kinase-like domain and a catalytic domain. It is expressed as two differentially glycosylated forms, a 130 kDa precursor form present in the endoplasmic reticulum and a 145 kDa form present on the plasma membrane. Ligand binding to the extracellular domain of GC-C promotes the accumulation of cGMP. GC-C acts as the receptor for heatstable enterotoxins, small peptides secreted by some pathogenic strains of E. coli that cause severe secretory diarrhea. GC-C also binds to guanylin and uroguanylin peptides, which modulate renal function in response to oral salt load.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
