Preservative: None Constituents: Glycerol, Sodium chloride, HEPES
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Synthetic C-terminal peptide (EIAAFQRRKAERQLVRNKP) corresponding to unique amino acid sequences on Particulate Guanylyl Cyclase F protein.
Immunogen affinity purified
The antibodies are affinity purified against immobilized antigen based affinity chromatography which yielded epitope-specific antibodies.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Guanylate Cyclase 2F,Gucy2F
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, sGC contains a heme group and binds NO that activates the enzyme, while particulate GC is stimulated by natriuretic peptides. Membrane-bound guanylyl cyclases (GCs) are peptide hormone receptors whereas the cytosolic isoforms are receptors for nitric oxide. Particulate GC (PGCs) have 7 different isoforms, PGCA through PGCG and are expressed in most tissues in isoform specific manner. Plasma membrane forms of guanylyl cyclase have been shown to function as natriuretic peptide receptors. In response to G-protein couples receptor stimulation, the cGMP can be produced from GTP by either cytoplasmic, soluble guanylate cyclase (sGC) are heterodimers, 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. 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). Two cDNA clones isolated from rat eye cDNA library encodes for two membranes associated guanylate cyclase E and F. The expression of PGCF is confined to eye, none of the ligand kown to stimulate other guanylate cyclases failed to stimulate PGCE and F subtype. Tus both PGCE and PGCF are considered as orphan receptors. The PGCF structure resembles most closely with other sensory PGC isoforms, the conservations are in the intracellular kinase like and catalytic domains, and is most divergent at N and C terminal regions. The PGCF is expressed only in retina. It is suggested that membrane receptor GCs may be involved in the control of inner ear electrolyte and fluid composition whereas NO stimulated GC isoforms mainly participate in the regulation of blood flow and supporting cell physiology. At present PGC-E and PGCF ligands are not known and they fall under Orphan Receptor category.