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Guanylate Cyclase ?1 subunit (soluble) Polyclonal Antibody

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    Guanylate Cyclase ?1 subunit (soluble) Polyclonal Antibody
  • Guanylate Cyclase ?1 subunit (soluble) Polyclonal Antibody
Cat No: 160897
Cayman

Soluble guanylate cyclase (sGC) is a heterodimeric hemoprotein and nitric oxide (NO) sensor composed of two subunits, α1 and β1.{59045,59046} The approximately 70 kDa sGC β1 subunit is encoded by GUCY1B3 in humans, ubiquitously expressed, and localize...

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: 1 ea

This product can only be bought through Cayman Chemical. Please contact us.

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • guanylyl GCS?1 GCS-?1 GCS-?-1 Gucy-1b1 hetero dimer hemo protein Gucy-1B3 immuno histochemistry
Product Overview:
Soluble guanylate cyclase (sGC) is a heterodimeric hemoprotein and nitric oxide (NO) sensor composed of two subunits, α1 and β1.{59045,59046} The approximately 70 kDa sGC β1 subunit is encoded by GUCY1B3 in humans, ubiquitously expressed, and localized to the cytosol.{24381} The sGC histidine residue at position 105 is ligated to a ferrous heme that selectively binds NO to activate the C-terminal guanylate cyclase activity of the sGC heterodimer, catalyzing the synthesis of cGMP.{59045,59047} Knockdown of Gucy1B3 or expression of a heme-deficient sGC β1 subunit inhibits NO-induced reductions in blood pressure and platelet activation in mice, indicating a heme-dependent role for the sGC β1 subunit in blood pressure regulation.{59048} Cayman’s Guanylate Cyclase β1 subunit (soluble) Polyclonal Antibody can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes the sGC β1 subunit from human, bovine, and rat samples.
Size 1 ea
Shipping dry ice
Host Rabbit
Antigen Synthetic peptide from an internal region of rat sGC ?1 subunit
Application(s)

IHC and WB

Formulation 500 µl of peptide affinity-purified polyclonal antibody
Custom Code 3822.19
UNSPSC code 12352203

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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