Guanylyl cyclase α1β1 (soluble) (human), (recombinant) (His-tag) (purified)
Product Details
Alternative Name: | GTP pyrophosphate-lyase (cycling), sGCα1/sGCβ1 |
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MW: | ~70kDa/~86kDa / subunit, respectively; heterodimer. |
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Source: | Produced in Sf9 insect cells. Fused at the C-terminus to a His-tag. Produced in a baculovirus expression system. |
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EC: | 4.6.1.2 |
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UniProt ID: | Q02108 (GCα1), Q02153 (GCβ1) |
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Formulation: | Liquid. In 50 mM Triethanolamine, pH 7.4, containing 150 mM NaCl, and 25% glycerol. |
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Purity: | ≥90% (SDS-PAGE) |
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Specific Activity: | Basal: ≥0.050 µmol/mg/min. - 100µM DEA NONOate (Prod. No. ALX-430-034) ≥10 µmol/mg/min. |
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Application Notes: | Biophysical and enzymatic studies and drug screening. |
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Shipping: | Shipped on Dry Ice |
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Long Term Storage: | -80°C |
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Use/Stability: | We do not recommend to store for longer periods after opening and thawing of the product. |
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Handling: | Avoid freeze/thaw cycles. |
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Scientific Background: | Guanylyl cyclase is part of the G protein signaling cascade that is activated by low intracellular calcium levels and inhibited by high intracellular calcium levels. In response to calcium levels, guanylyl cyclase synthesizes cGMP from GTP. cGMP keeps cGMP-gated channels open, allowing for the entry of calcium into the cell. |
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Regulatory Status: | RUO - Research Use Only |
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Figure: Spectral characteristics of basal and NO-treated purified human sGCα1β1 (3µM). Inset – Coomassie staining of 3µg of purified sGCα1β1. PM- protein marker.
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Product Literature References
A new small molecule inhibitor of soluble guanylate cyclase: F. Mota, et al.; Bioorg. Med. Chem. 23, 5303 (2015), Abstract; Full Text
Surface plasmon resonance using the catalytic domain of soluble guanylate cyclase allows the detection of enzyme activators: F. Mota, et al.; Bioorg. Med. Chem. Lett. 24, 1075 (2014), Abstract; Full Text
Abacavir increases platelet reactivity via competitive inhibition of soluble guanylyl cyclase: P.D. Baum, et al.; AIDS 25, 2243 (2011), Application(s): Assay, Abstract; Full Text
Inhibition of nitric oxide-activated guanylyl cyclase by calmodulin antagonists: L.R. James, et al.; Br. J. Pharmacol. 158, 1454 (2009), Abstract; Full Text
Nitric oxide production from nitrite occurs primarily in tissues not in the blood: critical role of xanthine oxidase and aldehyde oxidase: H. Li, et al.; J. Biol. Chem. 283, 17855 (2008), Abstract; Full Text
Human soluble guanylate cyclase: functional expression, purification and structural characterization: D.N. Kosarikov, et al.; Arch. Biochem. Biophys. 388, 185 (2001), Abstract;
Human recombinant soluble guanylyl cyclase: expression, purification, and regulation: Y.C. Lee, et al.; PNAS 97, 10763 (2000), Abstract; Full Text
Purified soluble guanylyl cyclase expressed in a baculovirus/Sf9 system: stimulation by YC-1, nitric oxide, and carbon monoxide: M. Hoenicka, et al.; J. Mol. Med. 77, 14 (1999), Abstract;
Human soluble guanylate cyclase: functional expression and revised isoenzyme family: U. Zabel, et al.; Biochem. J. 335 (Pt 1), 51 (1998), Abstract; Full Text
Soluble guanylate cyclase purified from bovine lung contains heme and copper: R. Gerzer, et al.; FEBS Lett. 132, 71 (1981), Abstract;
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