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Key Documents

G4405

Sigma-Aldrich

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

enhanced validation

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-GC-S-beta-1, Anti-GC-SB3, Anti-GUC1B3, Anti-GUCB3, Anti-GUCSB3, Anti-GUCY1B3

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 70 kDa

Espèces réactives

rat, mouse, human, bovine

Validation améliorée

independent
Learn more about Antibody Enhanced Validation

Technique(s)

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

Description générale

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

Immunogène

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.

Application

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.

Actions biochimiques/physiologiques

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.
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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Staffan Hildebrand et al.
Communications biology, 5(1), 197-197 (2022-03-05)
The nitric oxide-cGMP (NO-cGMP) pathway is of outstanding importance for vascular homeostasis and has multiple beneficial effects in vascular disease. Neointimal hyperplasia after vascular injury is caused by increased proliferation and migration of vascular smooth muscle cells (VSMCs). However, the
Allyson G Hindle et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 316(6), R704-R715 (2019-03-21)
Nitric oxide (NO) is a potent vasodilator, which improves perfusion and oxygen delivery during tissue hypoxia in terrestrial animals. The vertebrate dive response involves vasoconstriction in select tissues, which persists despite profound hypoxia. Using tissues collected from Weddell seals at
Oxygen Binding and Redox Properties of the Heme in Soluble Guanylate Cyclase IMPLICATIONS FOR THE MECHANISM OF LIGAND DISCRIMINATION
Makino R, et al.
The Journal of Biological Chemistry, 286(18), 15678-15687 (2011)
S Iino et al.
Neuroscience, 152(2), 437-448 (2008-02-19)
Nitric oxide (NO) is a major signaling molecule in the gastrointestinal tract, and released NO inhibits muscular contraction. The actions of NO are mediated by stimulation of soluble guanylate cyclase (sGC, NO-sensitive GC) and a subsequent increase in cGMP concentration.
A Vazquez-Torres et al.
Infection and immunity, 64(8), 3127-3133 (1996-08-01)
Nitric oxide (NO) is associated with functions as diverse as peristalsis, blood flow, neuroendosecretion, visual transduction, smooth muscle relaxation, and microbial killing (H. H. W. H. Schmidt and V. Walter, Cell 78:919-925, 1994). Despite the well-established role of NO in

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