| Product Name | Recombinant Rat Cytochrome P450 1B1 (Cyp1b1) |
|---|---|
| Description | Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. |
| Synonyms |
CYPIB1 Cytochrome P450RAP |
| Host | E.coli |
| Molecular Weight | 64.6 |
| Amino Acid Sequence | MATSLSADSPQQLSSLSTQQTILLLLVSVLAIVHLGQWLLRQWRRKPWSSPPGPFPWPLIGNAASVGRASHLYFARLARRYGDVFQIRLGSCPVVVLNGESAIHQALVQQGGVFADRPPFASFRVVSGGRSLAFGHYSERWKERRRAAYGTMRAFSTRHPRSRGLLEGHALGEARELVAVLVRRCAGGACLDPTQPIIVAVANVMSAVCFGCRYNHDDAEFLELLSHNEEFGRTVGAGSLVDVMPWLQLFPNPVRTIFREFEQINRNFSNFVLDKFLRHRESLVPGAAPRDMMDAFILSAEKKATGDPGDSPSGLDLEDVPATITDIFGASQDTLSTALLWLLILFTRYPDVQARVQAELDQVVGRDRLPCMSDQPNLPYVMAFLYESMRFTSFLPVTLPHATTANTFVLGYYIPKNTVVFVNQWSVNHDPAKWSNPEDFDPARFLDKDGFINKALASSVMIFSVGKRRCIGEELSKTLLFLFISILAHQCNFKANQNEPSNMSFSYGLSIKPKSFKIHVSLRESMKLLDSAVEKLQAEEACQ |
| Protein Length | Full Length, 1-543aa |
| Tag | N-terminal 6xHis-tagged |
| Reactivity | Rat |
| Applications | SDS-PAGE |
| Form | Liquid, in Tris-based buffer, 50% glycerol |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| References | "Specificity determinants of CYP1B1 estradiol hydroxylation."Nishida C.R., Everett S., Ortiz de Montellano P.R.Mol. Pharmacol. 84:451-458(2013) |
| Background | Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. |
| Supplier | Cusabio |
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