Specification
Description | Recombinant protein from the full-length sequence of Homo sapiens cytochrome P450 family 2 subfamily J member 2 (CYP2J2), transcript variant 1 (NM_000775). |
Organism | Homo sapiens (Human) |
Expression Host | Human Cells |
Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
Purity | Greater than 90% by SDS-PAGE gel |
Uniprot ID | P51589 |
Entry Name | CP2J2_HUMAN |
Gene Names | CYP2J2 |
Alternative Gene Names | |
Alternative Protein Names | Cytochrome P450 2J2 (EC 1.14.14.-) (Albendazole monooxygenase (hydroxylating)) (EC 1.14.14.74) (Albendazole monooxygenase (sulfoxide-forming)) (EC 1.14.14.73) (Arachidonic acid epoxygenase) (CYPIIJ2) (Hydroperoxy icosatetraenoate isomerase) (EC 5.4.4.7) |
Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
Length | 502 |
Molecular Weight(Da) | 57611 |
Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVDFEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHIFKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDPHFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFLPGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMPYTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDTFNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLSLKFRMGITISPVSHRLCAVPQV |
Background
Function | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system (PubMed:8631948, PubMed:19965576). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:8631948, PubMed:19965576). Catalyzes the epoxidation of double bonds of PUFA (PubMed:8631948, PubMed:19965576). Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools (PubMed:8631948). In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15-lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent (PubMed:19737933). Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone (PubMed:19923256). Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole (PubMed:23959307). Catalyzes the sulfoxidation of fenbedazole (PubMed:19923256). {ECO:0000269|PubMed:19737933, ECO:0000269|PubMed:19923256, ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:23959307, ECO:0000269|PubMed:8631948}. |
Pathway | Lipid metabolism; arachidonate metabolism. |
Protein Families | Cytochrome P450 family |
Tissue Specificity | Highly expressed in heart, present at lower levels in liver, kidney and skeletal muscle (at protein level). {ECO:0000269|PubMed:8631948}. |
QC Data
Note | Please contact us for QC Data |
Product Image (Reference Only) | ![]() |