Anti-Guanylyl Cyclase α1 antibody produced in rabbit

Description

• 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+.
• Physical form: Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
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