Anti-CYB5R3 Antibody Picoband® Fluoro488 Conjugated

NADH-cytochrome b5 reductase 3 is an enzyme that in humans is encoded by the CYB5R3 gene. This gene encodes cytochrome b5 reductase, which includes a membrane-bound form in somatic cells (anchored in the endoplasmic reticulum, mitochondrial and other membranes) and a soluble form in erythrocytes. The membrane-bound form exists mainly on the cytoplasmic side of the endoplasmic reticulum and functions in desaturation and elongation of fatty acids, in cholesterol biosynthesis, and in drug metabolism. The erythrocyte form is located in a soluble fraction of circulating erythrocytes and is involved in methemoglobin reduction. The membrane-bound form has both membrane-binding and catalytic domains, while the soluble form has only the catalytic domain. Alternate splicing results in multiple transcript variants. Mutations in this gene cause methemoglobinemias.

In developing embryos, expressed mainly in the choroid plexus, paraventricular neuroepithelium, placenta and kidney glomeruli. Also found in bronchial epithelium, adrenal gland and in seminiferous tubules of testis. High expression of VEGF continues in kidney glomeruli and choroid plexus in adults.

Ligand for members of the frizzled family of seven transmembrane receptors (Probable) . Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a role in normal ectoderm development. Required for normal tooth development. Required for normal postnatal development and maintenance of tongue papillae and sweat ducts. Required for normal proliferation of basal cells in tongue filiform papillae, plantar epithelium and sweat ducts. Required for normal expression of keratins in tongue papillae. Required for normal expression of KRT9 in foot plant epithelium. Required for normal hair follicle function.

1. Aalfs, C. M., Salieb-Beugelaar, G. B., Wanders, R. J. A., Mannens, M. M. A. M., Wijburg, F. A. A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: determination of the molecular basis. Hum. Mutat. 16: 18-22, 2000. 2. Board, P. G., Pidcock, M. E. Methaemoglobinaemia resulting from heterozygosity for two NADH-methaemoglobin reductase variants: characterization as NADH-ferricyanide reductase. Brit. J. Haemat. 47: 361-370, 1981. 3. Bull, P. C., Shephard, E. A., Povey, S., Santisteban, I., Phillips, I. R. Cloning and chromosomal mapping of human cytochrome b (5) reductase (DIA1) . Ann. Hum. Genet. 52: 263-268, 1988.