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Protoporphyrin IX (free acid)

Guanylyl cyclase activator
 
ALX-430-041-M300 300 mg 71.00 USD
 
ALX-430-041-G001 1 g 227.00 USD
Do you need bulk/larger quantities?
 
Replaces Prod. #: BML-CN230

Protoporphyrin IX free acid, as distinct from its zinc salt (which inhibits heme oxygenase), activates soluble guanylyl cyclase (sGC) by binding directly to the enzyme. A useful reagent in cases where the use of nitric oxide (NO) or nitric oxide donors is undesirable.

Product Details

Alternative Name:8,13-Divinyl-3,7,12,17-tetramethyl-21H,23H-porphine-2,18-dipropionic acid
 
Formula:C34H34N4O4
 
MW:562.7
 
CAS:553-12-8
 
MI:14: 7897
 
Purity:≥95% (HPLC)
 
Identity:Determined by NMR and UV/VIS.
 
Appearance:Purple to dark brown solid.
 
Solubility:Dissolve initially in 0.1M base (Tris base or NaOH), then add water miscible organic solvent (EtOH (10mg/ml), MeOH, DMSO (10mg/ml), DMF) until solution is 50/50 base/solvent. When a clear solution is obtained, it can be diluted into an aqueous medium and titrated or buffered to any pH>7. Use immediately.
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Use/Stability:Make solutions fresh daily.
 
Handling:Protect from light.
 
Regulatory Status:RUO - Research Use Only
 
430-041
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Product Literature References

Immune responses in beta-thalassaemia: heme oxygenase 1 reduces cytokine production and bactericidal activity of human leucocytes: A. Nithichanon, et al.; Sci. Rep. 10, 10297 (2020), Abstract; Full Text
Photodynamic intramolecular crosslinking of myoglobin: J. van Steveninck & T.M.A.R. Dubbelman; Biochim. Biophys. Acta 791, 98 (1984),
Porphyrins and chlorophylls as probes for fluoroimmunoassays [letter]: J.L. Hendrix; Clin. Chem. 29, 1003 (1983), Abstract;
Guanylate cyclase from bovine lung. A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme, and nitrosyl-heme: M.S. Wolin, et al.; J. Biol. Chem. 257, 13312 (1982), Abstract; Full Text
Model studies on photodynamic cross-linking: H. Verweij & J. Van Steveninck; Photochem. Photobiol. 35, 265 (1982), Abstract;

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