Skip to Content
Merck
All Photos(3)

Key Documents

G4280

Sigma-Aldrich

Anti-Guanylyl Cyclase α1 antibody produced in rabbit

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-GC-S-alpha-1, Anti-GC-SA3, Anti-GCS-alpha-3, Anti-GUC1A3, Anti-GUCA3, Anti-GUCSA3, Anti-GUCY1A3, Anti-MYMY6

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~80 kDa

species reactivity

mouse, rat, human, bovine

packaging

antibody small pack of 25 μL

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using trypsin-treated human, bovine and mouse heart tissue
immunoprecipitation (IP): 5-10 μg using 60-120 μg of a cytosolic fraction of rat brain
western blot: 1:10,000 using cytosolic fraction of rat brain

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

Disclaimer

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Gary W Wilson et al.
The European journal of neuroscience, 31(11), 1935-1945 (2010-06-10)
Most biological effects of nitric oxide (NO) in the brain are mediated by guanylyl cyclase-coupled NO receptors, whose activation results in increased intracellular cGMP levels. Apart from protein kinase activation little is known about subsequent cGMP signal transduction. In optic
Soluble guanylate cyclase: the forgotten sibling
Hobbs AJ
Trends in Pharmacological Sciences, 18(12), 484-491 (1997)
S Iino et al.
Neurogastroenterology and motility : the official journal of the European Gastrointestinal Motility Society, 21(5), 542-550 (2009-01-30)
Nitric oxide (NO) is an inhibitory signalling molecule in the gastrointestinal (GI) tract that is released from neurons and from leucocytes during inflammation. NO stimulates soluble guanylate cyclase (sGC), elevates cyclic guanosine 3',5'-monophospate (cGMP), and subsequently activates cGMP-dependent protein kinase
M Oppermann et al.
British journal of pharmacology, 155(3), 335-342 (2008-07-01)
The regulation of vascular soluble guanylyl cyclase (sGC) expression by nitric oxide (NO) is still under discussion. In vitro, NO has been shown to downregulate the expression of sGC but it is unclear if this mechanism is operative in vivo
Gwennan André et al.
Journal of the American Heart Association, 3(3), e000852-e000852 (2014-06-19)
Increasing evidence implicates overactivation of RhoA as a critical component of the pathogenesis of hypertension. Although a substantial body of work has established that Rac1 functions antagonize RhoA in a broad range of physiological processes, the role of Rac1 in

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service