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Merck

C3860

Sigma-Aldrich

Cytochrome P450 human

1B1 Isozyme Microsomes, with P450 Reductase, recombinant, expressed in baculovirus infected insect cells (BTI-TN-5B1-4)

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About This Item

Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12161501
NACRES:
NA.47

biological source

human

Quality Level

recombinant

expressed in baculovirus infected insect cells (BTI-TN-5B1-4)

form

solution

mol wt

45-60 kDa

packaging

vial of 0.5 nmol

suitability

suitable for molecular biology

UniProt accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... CYP1B1(1545)

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General description

Research Area: Immuno and CKS
Cytochromes are a type of protein belonging to superfamilies containing heme as a cofactor, making them hemoproteins. These proteins, also known as CYPs, serve as substrates in enzymatic reactions. The term "P450" originates from the enzyme′s maximum optical density peak at 450 nm when in its reduced state combined with carbon monoxide. Cytochromes are present in various tissues throughout the human body, with a predominant presence in intestinal and hepatic tissues.

Application

Cytochrome P450 human has been used in aflatoxin B1 (AFB1) metabolites analysis to study its effects on AFB1-induced cytotoxicity and micronuclei formation in human hepatocyte (L-02) and human lymphoblastoid (TK6) cells. It has also been used in cell-free cytochrome P4501B1 (CYP1B1) inhibition assays.

Biochem/physiol Actions

Cytochromes play a crucial role in metabolizing a wide range of xenobiotic compounds and are engaged in diverse functions such as steroid metabolism, deactivation of drugs and procarcinogens, metabolism of fatty acids, detoxification of xenobiotic substances, and breakdown of exogenous compounds. It facilitates the oxidation of substances using iron. CYP is well-established that changes in CYP enzymes often occur as a common consequence of immune system activation following infection and inflammation. Despite the overlapping effects of cytokines, the activity of human P450s is independently regulated in infection and inflammation.
Cytochrome P450 is a heterogeneous family of isozymes whose primary function is to oxidize small molecules, both as a function of intermediary metabolism (e.g., fatty acids) and to detoxify exogenous compounds (drugs or toxins). Some isoforms have narrow substrate specificity, while others are promiscuous. The CYP1A1 isoform catalyzes 7-deethylation of ethoxyresorufin. Cytochrome P450 (CYP) plays an important role in detoxifying xenobiotics, cellular metabolism and homeostasis. One of the main mechanisms of drug-drug interactions is the induction or inhibition of these enzymes. CYP enzymes are transcriptionally activated by a variety of xenobiotics and by endogenous substrates via receptor-dependent pathways. Inhibition of these enzymes is a major factor in metabolism-based drug-drug interactions, and many chemotherapeutic medications can cause drug interactions by either inhibiting or inducing the cytochrome p450 enzyme system.

Unit Definition

One unit will reduce 1 nanomole of cytochrome C per minute at pH 7.4 at 37 deg C.

Physical form

Solution in 100 mM potassium phosphate buffer, pH 7.4.

Preparation Note

Microsomes containing human CYP1B1 and recombinant human NADPH-P450 reductase.

Analysis Note

Tested for the ability to catalyze the 7-deethylation of ethoxyresorufin.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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The present study characterized in vitro metabolites of 20(R)-25-methoxyl-dammarane-3β, 12β, 20-triol (20(R)-25-OCH3-PPD) in mouse, rat, dog, monkey and human liver microsomes. 20(R)-25-OCH3-PPD was incubated with liver microsomes in the presence of NADPH. The reaction mixtures and the metabolites were identified
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Diosbulbin B (DIOB), a furan-containing diterpenoid lactone, is the most abundant component of Dioscorea bulbifera L. (DB), a traditional Chinese medicine herb. Administration of purified DIOB or DB extracts has been reported to cause liver injury in animals. The mechanisms

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