Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

COX5B Human

Cytochrome C Oxidase Subunit Vb Human Recombinant

Recombinant human COX5B, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 121 amino acids (32-129a.a). With a molecular mass of 13 kDa, COX5B is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26365
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

CYB5R3 Human

Cytochrome B5 Reductase 3 Human Recombinant

Recombinant human CYB5R3, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 34.0 kDa. It consists of 300 amino acids (27-301) and includes a 25 amino acid His-tag fused at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26656
Source
E.coli.
Appearance
Sterile filtered solution with a yellowish tint.

SCO2 Human

SCO Cytochrome Oxidase Deficient Homolog 2 Human Recombinant

Produced in E. coli, SCO2 is a single, non-glycosylated polypeptide chain comprising 246 amino acids (42-266a.a.) with a molecular weight of 27.4kDa. This protein is fused to a 21 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27140
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

CYP2D6

Cytochrome P450 2D6 Human Recombinant

Cytochrome P450 2D6 Human Recombinant, also known as liver/kidney microsomal antigen 1 (LKM1), is produced in SF9 insect cells. This glycosylated polypeptide has a molecular weight of 60 kDa and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26739
Source
Sf9 insect cells.
Appearance
Sterile, filtered liquid solution.

CYP2E1 Human

Cytochrome P450 2E1 Human Recombinant

CYP2E1 Human Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 488 amino acids (29-493 a.a.) with a molecular weight of 56.2 kDa. It features a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26820
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

POR (43-677) Human

P450 Oxidoreductase Human Recombinant

POR Human Recombinant, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain (amino acids 43-677) with a total of 642 amino acids and a molecular mass of 73.0 kDa. It includes a 6 amino acid His-tag fused at the C-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26922
Source
Sf9, Baculovirus cells.
Appearance
Sterile, colorless solution.

POR Human

P450 Oxidoreductase Human Recombinant

Produced in Sf9 Baculovirus cells, POR is a single, glycosylated polypeptide chain consisting of 686 amino acids (1-680a.a.) with a molecular weight of 77.9kDa. A 6-amino acid His tag is present at the C-terminus, and purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26998
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

POR Human, Active

P450 Oxidoreductase Human Recombinant, Active

Produced in Sf9 Baculovirus cells, POR is a single, glycosylated polypeptide chain. It consists of 686 amino acids (specifically, amino acids 1 through 680) and has a molecular weight of 77.9 kDa. For purification using proprietary chromatographic techniques, POR is expressed with a 6-amino acid His tag located at the C-terminus.
Shipped with Ice Packs
Cat. No.
BT27053
Source
Sf9, Baculovirus cells.
Appearance
The product is a clear solution that has undergone sterile filtration and appears colorless.

CYB5A Human

Cytochrome B5 Type A Human Recombinant

Recombinant human CYB5A, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 132 amino acids (with amino acids 1 to 108 being the actual CYB5A sequence) and has a molecular weight of 14.9 kDa. A 24-amino acid His-tag is fused to the N-terminus of CYB5A for purification purposes, which is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26434
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CYB5A Human, Sf9

Cytochrome B5 Type A, Sf9 Human Recombinant

CYB5A, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 117 amino acids (specifically, amino acids 1 to 108a.a.). Its molecular weight is 13.3kDa. However, on SDS-PAGE analysis, the apparent molecular size ranges from 18kDa to 28kDa. This CYB5A protein is expressed with a 9 amino acid His tag located at the C-terminus. Purification is achieved using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT26573
Source

Sf9, Baculovirus cells.

Appearance
A sterile, colorless solution that has been filtered.
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 .

© Copyright 2024 Thebiotek. All Rights Reserved.