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Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Additionally we are shipping Histidyl TRNA Synthetase Antibodies (75) and Histidyl TRNA Synthetase Kits (4) and many more products for this protein.
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Human HARS Protein expressed in Escherichia coli (E. coli) - ABIN667221
OHanlon, Miller: Genomic organization, transcriptional mapping, and evolutionary implications of the human bi-directional histidyl-tRNA synthetase locus (HARS/HARSL). in Biochemical and biophysical research communications 2002
Show all 2 references for ABIN667221
Loss of function mutations in histidyl-tRNA synthetase cause a spectrum of inherited peripheral neuropathies
Data suggest that by comparing human and trypanosomatid histidyl-tRNA synthetases (HisRS) may provide opportunities for developing specific inhibitors of Trypanosoma brucei HisRS.
Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis.
Data indicate that higher anti-Jo1 levels were associated with disease severity in antisynthetase syndrome (ASS (show ASS1 Proteins)) patients.
Findings suggest that histidyl-tRNA synthetase (HARS) is associated with axonal peripheral neuropathy.
Study identified sequence variants in the known disease-causing genes SLC6A3 (show SLC6A3 Proteins) and FLVCR1 (show FLVCR1 Proteins), and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1 (show C7orf27 Proteins), SNIP1 (show SNIP1 Proteins), CRADD (show CRADD Proteins), and HARS.
genomic organization of the HARS locus and mapping of transcripts originating from a bi-directional promoter controlling the differential expression of these gene
Demonstrating histidyl-tRNA synthetase (Jo-1)-specific T cell responses represents a key step in establishing the hypothesis that Jo-1 drives T cell-mediated autoimmunity in Jo-1+ polymyositis.
the TSG101 (show TSG101 Proteins) interaction with HRS is a crucial step in endocytic down-regulation of mitogenic signaling and this interaction may have a role in linking the functions of early and late endosomes
A proteolytically sensitive conformation of HisRS exists in the lung, the target tissue associated with this autoantibody response.
AA 60-90 of HRS were absolutely required for in vitro as well as in vivo signaling via MyD88 (show MYD88 Proteins)-dependent TLR pathways to case myositis.
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. Several transcript variants encoding different isoforms have been found for this gene.
, histidine translase
, histidine--tRNA ligase, cytoplasmic
, histidine tRNA ligase
, histidyl-tRNA synthetase, cytoplasmic
, dead end homolog 1
, Histidyl-tRNA synthetase, cytoplasmic