ANTI-GUANYLATE CYCLASE A1

Uses

Anti-Guanylyl Cyclase α1 antibody produced in rabbit is suitable for immunohistochemistry at a working dilution of 1:100 using trypsin-treated human, bovine and mouse heart tissue and immunoprecipitation at 5-10μg concentration using 60-120μg of a cytosolic fraction of rat brain. It is also suitable for western blot analysis using cytosolic fraction of rat brain at a working dilution of 1:10,000.
It was used as a primary antibody for immunohistochemical:

• localization of α1 subunits of sGC (soluble guanylate cyclase) in the guinea pig gastrointestinal tract
• detection of expression of sGC in the vasculature of rat skeletal muscle
• localization of the functional subunit of NO receptors, sGCα1 in guinea pig caecum

General Description

The enzyme consists of α and β subunits of ~80kDa and ~70kDa respectively. Both the units are required for catalytic activity. The N-terminal domains of the subunits are essential for the stimulation of the enzyme by NO. Dimerization is mediated by the central portion of GC. The C-terminus domain of both subunits forms the catalytic domain.

Biochem/physiol Actions

Guanylyl cyclase (GC) catalyzes the conversion of guanosine-5′-triphosphate (GTP) to cyclic guanosine-3′,5-monophosphate (cGMP) and pyrophosphate. This reaction requires Mg2+ or Mn2+.