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AV44362

Sigma-Aldrich

Anti-POR (AB1) antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-CPR, Anti-CYPOR, Anti-DKFZp686G04235, Anti-FLJ26468, Anti-P450 (cytochrome) oxidoreductase, Anti-P450R

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

77 kDa

species reactivity

mouse, human, guinea pig, bovine, dog, rat, rabbit

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... POR(5447)

General description

P450 (cytochrome) oxidoreductase (POR, CγPOR, P450R) is an FAD and FMN microsome membrane-bound enzyme required for electron transfer to several cytochrome P450 enzymes, heme oxygenase(s), cytochrome b(5) and squalene monooxygenases. CγPOR is an essential electron donor to enzymes involved in cholesterol biosynthesis. Mutation of CγPOR have been linked to Antley-Bixler-like Syndrome (ABS).

Specificity

Anti-POR (AB1) polyclonal antibody reacts with bovine, human, mouse, rat, chicken, zebrafish, pig, canine, and rabbit P450 (cytochrome) oxidoreductases.

Immunogen

Synthetic peptide directed towards the middle region of human POR

Application

Anti-POR (AB1) polyclonal antibody is used to tag P450 (cytochrome) oxidoreductase for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of P450 (cytochrome) oxidoreductase in metabolic processes that depend upon electron transfer to P450 enzymes, heme oxygenases, cytochrom b5 and squalene monooxygenases.

Biochem/physiol Actions

POR is an endoplasmic reticulum membrane oxidoreductase with an FAD-binding domain and a flavodoxin-like domain. The protein binds two cofactors, FAD and FMN, which allow it to donate electrons directly from NADPH to all microsomal P450 enzymes. Mutations in this POR gene have been associated with various diseases, including apparent combined P450C17 and P450C21 deficiency, amenorrhea and disordered steroidogenesis, congenital adrenal hyperplasia and Antley-Bixler syndrome.This gene encodes an endoplasmic reticulum membrane oxidoreductase with an FAD-binding domain and a flavodoxin-like domain. The protein binds two cofactors, FAD and FMN, which allow it to donate electrons directly from NADPH to all microsomal P450 enzymes. Mutations in this gene have been associated with various diseases, including apparent combined P450C17 and P450C21 deficiency, amenorrhea and disordered steroidogenesis, congenital adrenal hyperplasia and Antley-Bixler syndrome. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Sequence

Synthetic peptide located within the following region: VVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTE

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Jin Wuk Lee et al.
Environmental toxicology, 29(9), 1032-1042 (2012-11-30)
Benzo(a)pyrene (BaP) is a polycyclic aromatic hydrocarbon that causes mutations and tumor formation. Zacco platypus is a sentinel species that is suitable for monitoring aquatic environments. We studied cytochrome P450 system (CYP system) expression and DNA adduct formation in the

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