Active • Host: E. coli • AA: 24-677 • Tag: C-terminal His • MW: 76.4 kDa
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NADPH Cytochrome P450 Reductase (human, recombinant)

Item No. 33015

Technical Information
Synonyms
  • CPR
  • CYPOR
  • NADPH Hemoprotein Reductase
  • NCPR
  • P450R
  • POR
Purity
≥90% estimated by SDS-PAGE
Source
Active recombinant human C-terminal His-tagged NADPH cytochrome P450 reductase expressed in E. coli
Amino Acids
24-677
MW
76.4 kDa
50 mM potassium phosphate, pH 7.6, with 10% glycerol
UniProt Accession №
P16435
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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

    NADPH cytochrome P450 reductase (POR) is a flavoprotein and key electron donor to cytochrome P450s (CYPs).1,2 It is composed of an N-terminal membrane anchor domain and FMN-binding domain, which is linked to a C-terminal FAD-binding domain and NADPH-binding domain and localized to the cytosolic side of the endoplasmic reticulum.3,1,4 POR transfers electrons from NADPH through FAD and FMN coenzymes into the iron of the prosthetic heme group of CYPs.3,1 Cortical levels of POR are increased in the APPswe/PSEN1dE9 transgenic mouse model of Alzheimer’s disease.5 Deficiency in POR is associated with ambiguous genitalia and the disruption of steroid metabolism in patients with Antley-Bixler syndrome.6 Cayman’s NADPH Cytochrome P450 Reductase (human, recombinant) can be used for enzyme activity assays.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Laursen, T., Jensen, K., and Møller, B.L. Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. Biochim. Biophys. Acta 1814(1), 132-138 (2011).

    2. Backes, W.L., and Kelley, R.W. Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. Pharmacol. Ther. 98(2), 221-233 (2003).

    3. Jensen, K., and Møller, B.L. Plant NADPH-cytochrome P450 oxidoreductases. Phytochemistry 71(2-3), 132-141 (2010).

    4. Barnaba, C., Gentry, K., Sumangala, N., et alThe catalytic function of cytochrome P450 is entwined with its membrane-bound nature. F1000Res. 6(F1000 Faculty Rev), 662 (2017).

    5. Yao, Y., Huang, J.-Z., Chen, L., et alIn vivo and in vitro studies on the roles of p38 mitogen-activated protein kinase and NADPH-cytochrome P450 reductase in Alzheimer’s disease. Exp. Ther. Med. 14(5), 4755-4760 (2017).

    6. Pandey, A.V., and Flück, C.E. NADPH P450 oxidoreductase: Structure, function, and pathology of diseases. Pharmacol. Ther. 138(2), 229-254 (2013).