For immunochemical detection of the sGC β1 subunit
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Guanylate Cyclase β1 subunit (soluble) Polyclonal Antibody

Item No. 160897

Technical Information
Synonyms
  • sGC β1 subunit
  • GCS-beta-1
  • Gucy1b1
Immunogen
Synthetic peptide from an internal region of rat sGC β1 subunit
500 µl of peptide affinity-purified polyclonal antibody
Storage Buffer
PBS, pH 7.2, with 50% glycerol and 0.02% sodium azide
Host
Rabbit
Applications
IHC and WB
Cross Reactivity
(-) sGC α1 subunit
Species Reactivity
(+) Human(+) Bovine(+) Rat
UniProt Accession №
P20595
Origin
Animal/Rabbit
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    Product Description

    Soluble guanylate cyclase (sGC) is a heterodimeric hemoprotein and nitric oxide (NO) sensor composed of two subunits, α1 and β1.1,2 The approximately 70 kDa sGC β1 subunit is encoded by GUCY1B3 in humans, ubiquitously expressed, and localized to the cytosol.3 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.1,4 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.5 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.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Karow, D.S., Pan, D., Davis, J.H., et alCharacterization of functional heme domains from soluble guanylate cyclase. Biochemistry 44(49), 16266-16274 (2005).

    2. Montfort, W.R., Wales, J.A., and Weichsel, A. Structure and activation of soluble guanylyl cyclase, the nitric oxide sensor. Antioxid. Redox Signal. 26(3), 107-121 (2017).

    3. Derbyshire, E.R., and Marletta, M.A. Structure and regulation of soluble guanylate cyclase. Annu. Rev. Biochem. 81, 533-559 (2012).

    4. Wobst, J., Rumpf, P.M., Dang, T.A., et alMolecular variants of soluble guanylyl cyclase affecting cardiovascular risk. Circ. J. 79(3), 463-469 (2015).

    5. Thoonen, R., Cauwels, A., Decaluwe, K., et alCardiovascular and pharmacological implications of haem-deficient NO-unresponsive soluble guanylate cyclase knock-in mice. Nat. Commun. 6, 8482 (2015).

    Product Citations

    Cheng, D., Talib, J., Stanley, C.P., et alInhibition of MPO (myeloperoxidase) attenuates endothelial dysfunction in mouse models of vascular inflammation and atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 39(7), 1448-1457 (2019).