CYPOR Antibody (F-10): sc-25270

CYPOR Antibody (F-10) is a mouse monoclonal IgG2b kappa light chain antibody that detects CYPOR protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). CYPOR (F-10) antibody is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. CYPOR protein, also known as cytochrome P450 reductase, plays a crucial role in the metabolism of diverse endogenous and xenobiotic compounds by facilitating electron transfer from NADPH to cytochrome P450 enzymes during their catalytic cycle. This electron transfer is essential for proper functioning of cytochrome P450 enzymes, which are involved in biotransformation of drugs and toxins, thereby influencing drug efficacy and toxicity. CYPOR is primarily localized in the endoplasmic reticulum, where CYPOR also interacts with other important proteins such as heme oxygenase and cytochrome b5, further underscoring significance in cellular metabolism. Structurally, CYPOR is related to two distinct flavoprotein families, ferredoxin nucleotide reductase and flavodoxin, and electron transfer activity depends on binding of two flavin cofactors, FAD and FMN, to respective domains. This intricate structure and function highlight CYPOR′s importance in maintaining metabolic homeostasis and potential implications in pharmacology and toxicology.

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CYPOR Antibody (F-10) References:

1. Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes.  |  Backes, WL. and Kelley, RW. 2003. Pharmacol Ther. 98: 221-33. PMID: 12725870
2. Mutations of human cytochrome P450 reductase differentially modulate heme oxygenase-1 activity and oligomerization.  |  Marohnic, CC., et al. 2011. Arch Biochem Biophys. 513: 42-50. PMID: 21741353
3. Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites.  |  Haniu, M., et al. 1989. Biochemistry. 28: 8639-45. PMID: 2513880
4. Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis.  |  Shen, AL., et al. 1989. J Biol Chem. 264: 7584-9. PMID: 2708380
5. Loss of Endothelial Cytochrome P450 Reductase Induces Vascular Dysfunction in Mice.  |  Malacarne, PF., et al. 2022. Hypertension. 79: 1216-1226. PMID: 35354305
6. Endothelial deletion of the cytochrome P450 reductase leads to cardiac remodelling.  |  Lopez, M., et al. 2022. Front Physiol. 13: 1056369. PMID: 36531184
7. Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states.  |  Vermilion, JL. and Coon, MJ. 1978. J Biol Chem. 253: 2694-704. PMID: 632295
8. Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and functional expression in yeast.  |  Ohgiya, S., et al. 1994. Biochim Biophys Acta. 1186: 137-41. PMID: 8011664
9. NADPH-P-450 reductase: structural and functional comparisons of the eukaryotic and prokaryotic isoforms.  |  Sevrioukova, IF. and Peterson, JA. 1995. Biochimie. 77: 562-72. PMID: 8589067
10. P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature.  |  Nelson, DR., et al. 1996. Pharmacogenetics. 6: 1-42. PMID: 8845856
11. Quantitation of FAD-dependent cytochrome P450 reductase activity by photoreduction.  |  Hodgson, AV. and Strobel, HW. 1996. Anal Biochem. 243: 154-7. PMID: 8954538
12. P450BM-3; a tale of two domains--or is it three?  |  Peterson, JA., et al. 1997. Steroids. 62: 117-23. PMID: 9029725

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-CYPOR Antibody (F-10) has 25 citations in a variety of scientific publications.

Primary antibodies like Anti-CYPOR Antibody (F-10) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

CYPOR Antibody (F-10) Specifications

Alternate Product Name: CYPOR

Product Clone Name: F-10

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2b kappa light chain

Amino Acids: 1-300

Epitope Target: CYPOR

Epitope Species: human

Product Reactivity/Detection: CYPOR

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, IHC(P), ELISA

Vialing Information: Each vial contains 200 µg IgG_2b kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 25 citations in various scientific publications

Available Conjugates/Forms for CYPOR Antibody (F-10): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin