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Biotinidase functions to recycle biotin in the body by cleaving biocytin (biotin-epsilon-lysine), a normal product of carboxylase degradation, resulting in regeneration of free biotin. Additionally we are shipping BTD Antibodies (45) and BTD Kits (9) and many more products for this protein.
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Human BTD Protein expressed in Human Cells - ABIN2006595
McMahon: Biotin in metabolism and molecular biology. in Annual review of nutrition 2002
Conserved seq in mammals, identification of putative gene for biotinidase in Drosophila
The common biotinidase gene mutations (p.R157H, p.D444H, c.98-104del7ins3, p.T532M) cumulatively accounted for 72.3% of all the mutant alleles in the Turkish population.
Summary of the demographic features of patients identified as biotinidase deficient from August of 2012 through August of 2013 and mutation analysis results for 20 cases in the southeast region of Turkey.
Three novel pathogenic variants in BTD gene were identified in a cohort of Brazilian patients with biotinidase deficiency and control suggesting an allelic heteregeneity of the condition.
Report incidence of profound biotinase deficiency in Swedish newborns and adoptive immigrant children.
High frequencies of biotinidase mutations may explain the high incidence of biotinidase deficiency in Hungary.
Mutation analysis revealed three novel mutations, c.del631C and c.1557T>G within exon 4 and c.324-325insTA in exon 3 in Biotinidase deficiency patients and families.
Six different mutations in the biotinidase gene are identified in biotinidase in four Chinese patients; determination of biotinidase activities are performed for selective screening of biotinidase deficiency
loss of overall biotinidase expression is a novel marker for thyroid cancer aggressiveness.
Plasma BTD activity increases in hepatic glycogen (show GYS1 Proteins) storage disease patients.
140 known mutations in the biotinidase gene (BTD) that cause biotinidase deficiency, are reported.
Biotinidase knockout mice show cellular energy deficit and altered carbon metabolism gene expression similar to that of nutritional biotin deprivation.
This study demonistrated that biotinidase deficiency mice showed demylination and axonal degeneration.
results indicate low expression of biotinidase throughout the brain, but increased concentrations within the dorsal cochlear nucleus, ventral cochlear nucleus, and superior olivary complex as well as in the hair cells and spiral ganglion of the cochlea
Biotinidase functions to recycle biotin in the body by cleaving biocytin (biotin-epsilon-lysine), a normal product of carboxylase degradation, resulting in regeneration of free biotin. Biotinidase has also been shown to have biotinyl-transferase activity. Defects in the biotinidase gene cause multiple carboxylase deficiency.