Anti-Guanylyl Cyclase β1 (ER-19) antibody produced in rabbit

MFCD03455078

NA.41

Soluble guanylyl cyclase (sGC) is an obligate hemoprotein enzyme consisting of α and β subunits of ~80 kDa and ~70 kDa, respectively.

synthetic peptide corresponding to amino acid residues 189-207, with N-terminal added lysine, of rat soluble guanylate cyclase 1, conjugated to KLH with glutaraldehyde. The sequence differs in human, bovine and mouse by 1 amino acid.

Anti-Guanylyl Cyclase β1 (ER-19) antibody produced in rabbit is suitable for immunoblotting at a working dilution of 1:2000 using a cytosolic fraction of rat brain, immunoprecipitation at a working antibody amount of 2-3μg using 60-120μg of a cytosolic fraction of rat brain and for immunohistochemistry at 1:400 using trypsin-digested human, bovine and mouse heart tissue.
It has been used as a primary antibody for:

• localization of β1 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, sGCβ1 in guinea pig caecum

It has also been used in immunoblot assay to determine whether there were changes in uterine vascular smooth muscle (UVSM) sGC expression during the ovine reproductive cycle.

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.
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⁺. 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.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

rabbit

200

unconjugated

affinity isolated antibody

primary antibodies

polyclonal

buffered aqueous solution

antigen 70 kDa

rat, human, bovine, mouse

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using trypsin-digested human, bovine and mouse heart tissue
immunoprecipitation (IP): 2-3 μg using 60-120 μg of a cytosolic fraction of rat brain
western blot: 1:2,000 using cytosolic fraction of rat brain

dry ice

−20℃

human ... GUCY1B3(2983)
mouse ... Gucy1b3(54195)
rat ... Gucy1b3(25202)

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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