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HLCS encodes an enzyme that catalyzes the binding of biotin to carboxylases and histones. Additionally we are shipping Biotin-Protein Ligase Antibodies (29) and Biotin-Protein Ligase Kits (2) and many more products for this protein.
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The transcriptional function of HCS was shown by in vitro pull down and in vivo co-immunoprecipitation assays to depend on its interaction with the histone deacetylases HDAC1 (show HDAC1 Proteins), HDAC2 (show HDAC2 Proteins) and HDAC7 (show HDAC7 Proteins)
Data suggest that direct interactions of HLCS (holocarboxylase synthetase) with NCOR1 (nuclear receptor corepressor 1 (show NCOR1 Proteins)) and HDAC1 (histone deacetylase 1 (show HDAC1 Proteins)) contribute toward transcriptional repression of repeats, presumably increasing genome stability.
study characterizes three functional promoters in the human HLCS gene
HLCS interacts physically with the DNA methyltransferase (show DNMT1 Proteins) DNMT1 (show DNMT1 Proteins) and the methyl CpG binding protein MeCP2 (show MECP2 Proteins) to facilitate the binding of HLCS to chromatin.
This study showed that modification of HSP72 (show HSPA1A Proteins) and demonstrated that binding of biotin to extracellular HSP72 (show HSPA1A Proteins) prepares cells for a strong immune response.
individuals with HLCS SNPs may benefit from supplemental biotin, yet to different extents depending on the genotype
HLCS methionine-58 is a functional translation start site in human cells.
Holocarboxylase synthetase interacts directly with histone H3 (show HIST3H3 Proteins), causing biotinylation of lysine K9 and K18 (show KRT18 Proteins).
Mutation analysis by polymerase chain reaction-sequencing of the entire coding region of the HLCS gene revealed the c.1522C>T (p.R508W) mutation in six of the eight mutant alleles. suggests it as the most common mutation in the Thai population
The results of this study suggest that miR (show MLXIP Proteins)-539 is among the factors sensing biotin and regulating holocarboxylase synthetase expression.
This gene encodes an enzyme that catalyzes the binding of biotin to carboxylases and histones. The protein plays an important role in gluconeogenesis, fatty acid synthesis and branched chain amino acid catabolism. Defects in this gene are the cause of holocarboxylase synthetase deficiency. Multiple alternatively spliced variants, encoding the same protein, have been identified.
biotin apo-protein ligase
, biotin- [propriony-Coenzyme A-carboxylase (ATP-hydrolysing)] ligase
, biotin--protein ligase
, biotin--[acetyl-CoA-carboxylase] ligase
, biotin--[methylcrotonoyl-CoA-carboxylase] ligase
, biotin--[methylmalonyl-CoA-carboxytransferase] ligase
, holocarboxylase synthetase (biotin-(proprionyl-Coenzyme A-carboxylase (ATP-hydrolysing)) ligase)
, holocarboxylase synthetase (biotin- [propriony-Coenzyme A-carboxylase (ATP-hydrolysing)] ligase)