ANTI-GUANYLYL CYCLASE ALPHA1 SOLUBLE DEVELOPED IN RABBIT IGG FRACTION OF ANTISERUM

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.

Immunogen

synthetic peptide corresponding to amino acid residues 673-690 of rat soluble Guanylyl cyclase α1, conjugated to KLH with glutaraldehyde. The corresponding human sequence differs by 2 amino acids.

Application

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

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⁺.

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⁺.†† The enzyme (GC) is a major physiological receptor for nitric oxide (NO), an important intra- and intercellular membrane-permeant signaling molecule. Gaseous NO binds to Fe²⁺ in the prosthetic heme group of the enzyme. NO binding is followed by disruption of the β1 subunit histidine¹⁰⁵ bond to iron and activation of the enzyme. GC forms a complex with NO and cGMP and regulates smooth muscle relaxation, inflammation, platelet adhesion and aggregation, pulmonary physiology and neuronal function. It is an important target for NO-releasing and non-NO-releasing activator drugs in human cardiovascular therapy.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

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