Histidyl-tRNA synthetase (HARS)

Full length E. coli Histidyl-tRNA synthetase (HARS) which has been purified using Q-sepharose and hydroxyapatite chromatography.

Histidyl-tRNA synthetases attach amino acids to the 3' ends of their cognate transfer RNAs in a two-step reaction catalyzed by ATP. The accuracy of this reaction is crucial for the overall fidelity of protein synthesis. Defects in HARS are a cause of Usher syndrome type 3B (USH3B) [MIM:614504]. USH3B is a syndrome characterized by progressive vision and hearing loss during early childhood. Some patients have the so-called 'Charles Bonnet syndrome,' involving decreased visual acuity and vivid visual hallucinations. USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH3 is characterized by postlingual, progressive hearing loss, variable vestibular dysfunction, and onset of retinitis pigmentosa symptoms, including nyctalopia, constriction of the visual fields, and loss of central visual acuity, usually by the second decade of life.

From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.

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Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EVM101
Histidyl-tRNA synthetase (HARS), 50ug
50ug In stock
Regular Price:$300.00
On Sale:
EVM108
Histidyl-tRNA synthetase (HARS), 100ug
100ug In stock
Regular Price:$475.00
On Sale:
EVM109
Histidyl-tRNA synthetase (HARS), 250ug
250ug In stock
Regular Price:$890.00
On Sale:
Specifications

Product Type: Protein
Name: Histidyl-tRNA Synthetase Recombinant Protein
Accession ID: AAC75567, P12081
Source: E. coli
Molecular Weight: 47 kDa
Amino Acid Sequence: makniqairgmndylpgetaiwqriegtlknvlgsygyseirlpiveqtplfkraigevtdvvekemytfedrngdsltlrpegtagcvragiehgllynqeqrlwyigpmfrherpqkgryrqfhqlgcevfglqgpdidaelimltarwwralgisehvtlelnsigslearanyrdalvafleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckllesagiaytvnqrlvrgldyynrtvfewvtnslgsqgtvcaggrydglveqlggratpavgfamglerlvllvqavnpefkadpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvavvlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
Purity: > 95% by Q-sepharose, hydroxyapatite
Buffer: 50 mM HEPES pH 7.5; 100 mM KCl; 10 mM MgCl2, 5 mM ?-mercaptoethanol, 40% glycerol
Concentration: 100 uM
Storage: Store at -20C
Shipped: Dry ice

Provider
From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.
Comments

See Franckyln, C., et al., JMB, (1994), for purification and crystallization procedures

References
  1. Francklyn, C. and Schimmel, P., Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. PNAS, 87, 8655-8659, (1990).
  2. Franckyln, C., Harris, D., and Moras, D., Crystallization of Histidyl-tRNA Synthase from Escherichia coli, JMB, 241, 275-277, (1994).

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