CYB5R1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 300 amino acids (29-305) and having a molecular mass of 33.8kDa. CYB5R1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Cytochrome B5 Reductase 1 is a NADH-dependent enzyme that catalyzes the reduction of cytochrome b5 from its ferric (Fe3+) to its ferrous (Fe2+) state . This reduction is critical for the enzyme’s role in various metabolic pathways, including:
CYB5R1 exists in multiple isoforms, which are produced through alternative splicing. These isoforms can be either soluble or membrane-bound, allowing the enzyme to function in different cellular compartments . The membrane-bound form is typically associated with the endoplasmic reticulum and the outer mitochondrial membrane, where it participates in electron transfer reactions .
Mutations or deficiencies in CYB5R1 can lead to various metabolic disorders. For instance, a deficiency in this enzyme can result in methemoglobinemia, a condition characterized by an increased level of methemoglobin in the blood, leading to reduced oxygen delivery to tissues . Understanding the structure and function of CYB5R1 is crucial for developing therapeutic strategies to treat such conditions.
Recombinant CYB5R1 is produced using genetic engineering techniques, where the human CYB5R1 gene is cloned and expressed in a suitable host system, such as bacteria or yeast. This recombinant enzyme is used in research to study its biochemical properties and potential therapeutic applications. The availability of human recombinant CYB5R1 allows for detailed studies on its structure, function, and role in various metabolic pathways, providing insights into its potential as a therapeutic target.