Detection of Human, Mouse, and Rat POR/ Cytochrome P450 Reductase by Western Blot.
Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line, mouse kidney tissue, and rat kidney tissue. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human/Mouse/Rat POR/Cytochrome P450 Reductase Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6340) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for POR/Cytochrome P450 Reductase at approximately 85 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Sterile PBS to a final concentration of 0.2 mg/mL.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: POR/Cytochrome P450 Reductase
NADPH-Cytochrome P450 Reductase (P450R) is an essential component of the cytochrome P450 monooxygenase system of eukaryotic cells (1). P450R is anchored in the endoplasmic reticulum membrane with its catalytic domain residing in the cytosol. P450R is a flavoprotein, containing one molecule each of FMN and FAD, which are essential for the transfer of electrons from NADPH to the cytochromes P450 (2). This reduction is necessary for cytochromes P450 to perform each cycle of oxidation. P450R is also capable of transferring electrons to cytochrome b5, heme oxygenase, the fatty acid elongation system, and other proteins. Mutations of P450R can result in disordered steroidogenesis and Antley-Bixler syndrome.
Philips, A.H. and R.G. Langdon (1962) J. Biol. Chem. 237:2652.
Iyanagi, T. and H.S. Mason (1973) Biochemistry 12:2291.
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