Recombinant Proteins

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Product List

COX5B Human

Cytochrome C Oxidase Subunit Vb Human Recombinant

COX5B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (32-129a.a) and having a molecular mass of 13kDa.
COX5B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26365
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CYB5A Human

Cytochrome B5 Type A Human Recombinant

CYB5A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (1-108 a.a) and having a molecular mass of 14.9kDa.
CYB5A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26434
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CYB5A Human, Sf9

Cytochrome B5 Type A, Sf9 Human Recombinant

CYB5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 117 amino acids (1-108a.a.) and having a molecular mass of 13.3kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).
CYB5A is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26573
Source

Sf9, Baculovirus cells.

Appearance
Sterile filtered colorless solution.

CYB5R3 Human

Cytochrome B5 Reductase 3 Human Recombinant

CYB5R3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 300 amino acids (27-301) and having a molecular mass of 34.0kDa.
CYB5R3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26656
Source
E.coli.
Appearance

Sterile filtered yellowish solution.

CYP2D6

Cytochrome P450 2D6 Human Recombinant

Cytochrome P450 2D6 Human Recombinant (also called liver/kidney microsomal antigen 1) produced in SF9, is a glycosylated, polypeptide chain having a molecular mass of 60 kDa. The LKM1 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26739
Source
Sf9 insect cells.
Appearance
Sterile filtered liquid formulation.

CYP2E1 Human

Cytochrome P450 2E1 Human Recombinant

CYP2E1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 488 amino acids (29-493 a.a) and having a molecular mass of 56.2kDa.
CYP2E1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26820
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

POR (43-677) Human

P450 Oxidoreductase Human Recombinant

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.

Shipped with Ice Packs
Cat. No.
BT26922
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

POR Human

P450 Oxidoreductase Human Recombinant

POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. 
POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26998
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

POR Human, Active

P450 Oxidoreductase Human Recombinant, Active

POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. 
POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27053
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

SCO2 Human

SCO Cytochrome Oxidase Deficient Homolog 2 Human Recombinant

SCO2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (42-266a.a.) and having a molecular mass of 27.4kDa.
SCO2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27140
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Introduction

Definition and Classification

Cytochromes are redox-active proteins containing a heme group with a central iron atom at its core. They play a crucial role in the electron transport chain and redox catalysis. Cytochromes are classified based on the type of heme and its mode of binding. The International Union of Biochemistry and Molecular Biology (IUBMB) recognizes four main classes: cytochromes a, b, c, and d .

Biological Properties

Cytochromes exhibit key biological properties such as electron transfer and catalysis by reduction or oxidation of their heme iron. They are expressed in various tissues and are found as both globular and membrane proteins. For instance, cytochrome c is involved in electron transfer from complex III to complex IV in oxidative phosphorylation . The tissue distribution of cytochromes varies, with significant presence in mitochondria and other cellular locations depending on their function .

Biological Functions

The primary biological function of cytochromes is to facilitate electron transfer during cellular respiration, which is vital for ATP production. Cytochromes also play roles in immune responses and pathogen recognition. For example, cytochrome c is involved in apoptosis, a process crucial for immune regulation and pathogen elimination .

Modes of Action

Cytochromes interact with other molecules and cells through their heme group, which can alternate between reduced (Fe²⁺) and oxidized (Fe³⁺) states. This redox activity allows cytochromes to transfer electrons efficiently. Cytochrome c, for instance, transfers electrons between complexes III and IV in the electron transport chain . Binding partners and downstream signaling cascades are essential for their function in cellular respiration and other metabolic processes .

Regulatory Mechanisms

The expression and activity of cytochromes are regulated through various mechanisms, including transcriptional regulation and post-translational modifications. Heavy metals, for example, can induce the expression of cytochrome P450 genes through an aryl hydrocarbon receptor-dependent mechanism . Post-translational modifications such as phosphorylation also play a role in modulating cytochrome activity .

Applications

Cytochromes have numerous applications in biomedical research, diagnostic tools, and therapeutic strategies. They are used to study electron transfer processes, develop biosensors, and design drugs targeting cytochrome-related pathways. Cytochrome P450 enzymes, for instance, are crucial in drug metabolism and are targeted in pharmacological research .

Role in the Life Cycle

Throughout the life cycle, cytochromes play essential roles from development to aging and disease. During development, they are involved in energy production and cellular differentiation. In aging, cytochrome function can decline, leading to reduced cellular respiration efficiency. In diseases such as cancer, cytochrome c-mediated apoptosis is a critical pathway for eliminating damaged cells .

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