Cytochrome C Oxidase Subunit Vb Human Recombinant
Cytochrome B5 Reductase 3 Human Recombinant
SCO Cytochrome Oxidase Deficient Homolog 2 Human Recombinant
Cytochrome P450 2D6 Human Recombinant
Cytochrome P450 2E1 Human Recombinant
P450 Oxidoreductase Human Recombinant
P450 Oxidoreductase Human Recombinant
P450 Oxidoreductase Human Recombinant, Active
Cytochrome B5 Type A Human Recombinant
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.
Sf9, Baculovirus cells.
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 .
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 .
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 .
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 .
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 .
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 .
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 .