Recombinant Rat Cytochrome P450 1B1 (CYP1B1) Protein (His)

Name: Recombinant Rat Cytochrome P450 1B1 (CYP1B1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09414P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Rat Cytochrome P450 1B1 (CYP1B1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q64678
Target Symbol	CYP1B1
Synonyms	Cyp1b1Cytochrome P450 1B1; EC 1.14.14.1; CYPIB1; Cytochrome P450RAP; Hydroperoxy icosatetraenoate dehydratase; EC 4.2.1.152
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MATSLSADSPQQLSSLSTQQTILLLLVSVLAIVHLGQWLLRQWRRKPWSSPPGPFPWPLIGNAASVGRASHLYFARLARRYGDVFQIRLGSCPVVVLNGESAIHQALVQQGGVFADRPPFASFRVVSGGRSLAFGHYSERWKERRRAAYGTMRAFSTRHPRSRGLLEGHALGEARELVAVLVRRCAGGACLDPTQPIIVAVANVMSAVCFGCRYNHDDAEFLELLSHNEEFGRTVGAGSLVDVMPWLQLFPNPVRTIFREFEQINRNFSNFVLDKFLRHRESLVPGAAPRDMMDAFILSAEKKATGDPGDSPSGLDLEDVPATITDIFGASQDTLSTALLWLLILFTRYPDVQARVQAELDQVVGRDRLPCMSDQPNLPYVMAFLYESMRFTSFLPVTLPHATTANTFVLGYYIPKNTVVFVNQWSVNHDPAKWSNPEDFDPARFLDKDGFINKALASSVMIFSVGKRRCIGEELSKTLLFLFISILAHQCNFKANQNEPSNMSFSYGLSIKPKSFKIHVSLRESMKLLDSAVEKLQAEEACQ
Expression Range	1-543aa
Protein Length	Full Length
Mol. Weight	64.6kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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). Exhibits catalytic activity for the formation of hydroxyestrogens from 17beta-estradiol (E2), namely 2- and 4-hydroxy E2. Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites. May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system. Additionally, displays dehydratase activity toward oxygenated eicosanoids including hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2. Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products. Plays an important role in retinal vascular development. Under ambient/hyperoxic O2 conditions, promotes angiogenesis and capillary morphogenesis of retinal endothelial cells and pericytes, likely by metabolizing the oxygenated products symptomatic of oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression.
Subcellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Mitochondrion.
Protein Families	Cytochrome P450 family
Database References	KEGG: rno:25426 STRING: 10116.ENSRNOP00000061222 UniGene: PMID: 29115507 Incense smoke exposure significantly induced the expression of CYP1A1, CYP1A2, and CYP1B1 mRNAs in both lung and liver tissues. PMID: 24557852 The influence of dietary lipids on the ontogeny of XMEs was also evaluated. mRNA and protein levels of phase I (CYP1A1, CYP1A2, and CYP1B1) and phase II (NAD(P)H:quinone acceptor oxidoreductase 1 and GSTP1) enzymes were analyzed. PMID: 25164943 Increased oxidative stress generated by CYP1B1 contributes to hypertension. PMID: 24477449 Diphenylarsinic acid induced the expression of CYP1B1 in the liver and caused oxidative DNA damage. PMID: 23999541 Luteinizing hormone upregulates CYP1B1 protein expression in rat R2C leydig cells. PMID: 21389345 Data suggest that CYP1B1 contributes to deoxycorticosterone-salt-induced hypertension and associated pathophysiological changes, most likely as a result of increased ROS production and ERK1/2 and p38 MAPK activity. PMID: 20852048 Data suggest that cytochrome P450 1B1 contributes to angiotensin II-induced hypertension and associated pathophysiological changes. PMID: 20805442 Cytochrome P450 1B1 catalyzes the conversion of 17-beta-estradiol (E2) to thecatechol estrogen metabolites 2-OH-E2 and 4-OH-E2 that have been postulated to be involved in mammary carcinogenesis. PMID: 12010864 the expressions of CYP1A1, CYP1B1 and ER-mRNA in rat ovarian tissues were examined throughout the estrous cycle to establish any correlation in the expressions of these mRNAs in rat ovary PMID: 12223220 cAMP induction was mediated either by a 189bp far upstream enhancer region (FUER, -5110 to -5298) or by a 230bp AhR-responsive enhancer region (AhER) (-797 to -1026) PMID: 12859982 While increasing AhR binding to both CYP1A1 and CYP1B1, 2,3,7,8-tetrachlorodibenzo-p-dioxin induced CYP1A1 mRNA in both a malignant and non-malignant line but increased only CYP1B1 mRNA in the malignant line PMID: 18059014 expression of CYP1B1 in hyperplasia, squamous cell carcinomas in situ, or in association with inflammation may increase the production of carcinogenic metabolites, which may promote esophageal tumorigenesis PMID: 18618592

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.