POR (43-677) Human
Greater than 95.0% as determined by SDS-PAGE.
Description
POR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated, polypeptide chain (43-677 a.a) containing a total of 642 amino acids, having a molecular mass of 73.0 kDa.
POR is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Product Specs
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MLFRKKKEEV PEFTKIQTLT SSVRESSFVE KMKKTGRNII VFYGSQTGTA EEFANRLSKD AHRYGMRGMS ADPEEYDLAD LSSLPEIDNA LVVFCMATYG EGDPTDNAQD FYDWLQETDV DLSGVKFAVF GLGNKTYEHF NAMGKYVDKR LEQLGAQRIF ELGLGDDDGN LEEDFITWRE QFWPAVCEHF GVEATGEESS IRQYELVVHT DIDAAKVYMG EMGRLKSYEN QKPPFDAKNP FLAAVTTNRK LNQGTERHLM HLELDISDSK IRYESGDHVA VYPANDSALV NQLGKILGAD LDVVMSLNNL DEESNKKHPF PCPTSYRTAL TYYLDITNPP RTNVLYELAQ YASEPSEQEL LRKMASSSGE GKELYLSWVV EARRHILAIL QDCPSLRPPI DHLCELLPRL QARYYSIASS SKVHPNSVHI CAVVVEYETK AGRINKGVAT NWLRAKEPAG ENGGRALVPM FVRKSQFRLP FKATTPVIMV GPGTGVAPFI GFIQERAWLR QQGKEVGETL LYYGCRRSDE DYLYREELAQ FHRDGALTQL NVAFSREQSH KVYVQHLLKQ DREHLWKLIE GGAHIYVCGD ARNMARDVQN TFYDIVAELG AMEHAQAVDY IKKLMTKGRY SLDVWSHHHH HH. |
Product Science Overview
P450 oxidoreductase (POR), also known as cytochrome P450 reductase, is a crucial enzyme in the electron transfer chain, facilitating the transfer of electrons from NADPH to cytochrome P450 enzymes and other heme proteins in the endoplasmic reticulum of eukaryotic cells . This enzyme plays a vital role in various biochemical processes, including drug metabolism, steroid biosynthesis, and the detoxification of xenobiotics.
The human POR gene is located on chromosome 7 (7q11.23) and consists of 16 exons . The exons 2-16 code for a 677-amino acid POR protein . The protein is a membrane-bound enzyme composed of four structural domains: the FMN-binding domain, the connecting domain, the FAD-binding domain, and the NADPH-binding domain . The FMN-binding domain is similar to the structure of FMN-containing protein flavodoxin, while the FAD-binding and NADPH-binding domains resemble those of flavoprotein ferredoxin-NADP+ reductase (FNR) .
POR is essential for the catalytic activity of all microsomal cytochrome P450 enzymes . It transfers electrons from NADPH to cytochrome P450 enzymes, which are involved in the metabolism of a wide range of substrates, including drugs, steroids, and other xenobiotics . The general scheme of electron flow in the POR/P450 system is: NADPH → FAD → FMN → P450 → O2 .
Mutations in the POR gene can lead to POR deficiency, a complex disorder affecting steroidogenesis and, in severe cases, causing skeletal malformations known as Antley-Bixler syndrome . The POR gene is highly polymorphic, with numerous single-nucleotide polymorphisms (SNPs) identified in different populations . These polymorphisms can affect drug metabolism and steroid biosynthesis, contributing to pharmacogenetic variation in drug response and variations in steroid synthesis .
Recombinant human POR can be expressed in various systems, including E. coli, for research and therapeutic purposes . The recombinant protein is used to study the effects of amino acid sequence variants on the activity of cytochrome P450 enzymes and to assess the impact of genetic polymorphisms on enzyme function .
