Recombinant Human CYB5R2 protein - BSA and Azide free is a Human Full Length protein, in the 1 to 276 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction (By similarity). Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).
NADH-cytochrome b5 reductase 2, b5R.2, CYB5R2
Recombinant Human CYB5R2 protein - BSA and Azide free is a Human Full Length protein, in the 1 to 276 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab180333 is purified using conventional chromatography techniques.
NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction (By similarity). Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
The CYB5R2 target also known as cytochrome b5 reductase 2 functions as an enzyme involved in electron transfer processes. It catalyzes the reduction of cytochrome b5 using NADH as an electron donor playing a critical role in the redox reactions. The molecular mass of CYB5R2 is approximately 34 kDa. This protein shows expression in multiple tissues including the liver and testis which suggests its widespread importance in cellular processes.
Cytochrome b5 reductase 2 facilitates fatty acid desaturation and elongation. This protein does not function alone but often participates as part of larger enzyme complexes. In particular CYB5R2 operates in electron transport processes that are essential for maintaining cellular oxidation-reduction balance. Its activity in these processes highlights its role in maintaining metabolic homeostasis.
CYB5R2 engages in fatty acid metabolism and lipid biosynthesis pathways. The protein collaborates with cytochrome P450 enzymes to contribute to lipid modification. These pathways play fundamental roles in energy storage and membrane structure which are necessary for cell function and survival. CYB5R2 shows interactivity with proteins such as CYB5A highlighting the intricate network of cellular electron transport.
Mutations or dysregulation in cytochrome b5 reductase 2 have associations with methemoglobinemia and certain cancers. Methemoglobinemia emerges due to the inability to effectively reduce methemoglobin to hemoglobin causing inefficient oxygen delivery to tissues. The connection with CYB5R2 in this disease involves its critical function in electron transfer. Additionally research indicates links between variations in CYB5R2 and prostate cancer emphasizing its role in cellular growth and proliferation alongside interactions with other proteins such as CYB5A.
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15% SDS-PAGE analysis of ab180333 (3μg).
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