G4280
Anti-Guanylyl Cyclase α1 antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
别名:
Anti-GC-S-alpha-1, Anti-GC-SA3, Anti-GCS-alpha-3, Anti-GUC1A3, Anti-GUCA3, Anti-GUCSA3, Anti-GUCY1A3, Anti-MYMY6
产品名称
Anti-Guanylyl Cyclase α1 antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
biological source
rabbit
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
Quality Level
Gene Information
human ... GUCY1A3(2982)
mouse ... Gucy1a3(60596)
rat ... Gucy1a3(497757)
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:
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.
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
常规特殊物品
此项目有
Shingo Kimura et al.
Scientific reports, 12(1), 21960-21960 (2022-12-20)
This study was to evaluate whether Low-energy shock wave therapy (LESW) improves ischemic-induced overactive bladder in rats and investigate its therapeutic mechanisms. Sixteen-week-old male Sprague-Dawley rats were divided into three groups: arterial injury (AI), AI with LESW (AI-SW), and control
Soluble guanylate cyclase: the forgotten sibling
Hobbs AJ
Trends in Pharmacological Sciences, 18(12), 484-491 (1997)
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.
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
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
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