
Histidyl tRNA synthetase
HisRS
Histidine tRNA ligase
Size: 0.2mg
Source: Calf Thymus
Catalogue Number: ATJ01-02
Product Information
Jo-1 autoantibodies are capable of inhibiting the activity of the target antigen (HRS) and can immunoprecipitate labelled enzyme as well as its specific tRNA. HRS has a molecular weight of 55 kDa in SDS-polyacrylamide electrophoresis, and is believed to exist as a dimer in its native state.
The amino acid sequence of human Jo-1 antigen has been determined by cloning and sequencing its cDNA. It contains three structural motifs typical of class IIa aminoacyl transferases and two signature regions common to histidyl-tRNA synthetases. The human enzyme amino acid sequence shows significant homology to those of the enzymes from yeast (47.5%) and E. coli. It is predicted to have a coiled-coil α-helical structure that is characteristic of many autoantigens and which contains the major autoantigenic epitope.
Clinical Indications
Polymyositis
Dermatomyositis
MSDS
References
Targoff, I.N. (1991) Curr. Prob. Dermatol. 3, 134
Plotz, P.H. et al. (1989) Ann. Int. Med. 111, 143
Reichlin, M. et al. (1984) Arthritis Rheum. 27, 1150
Nishikai, M., Reichlin, M. (1980) Arthritis Rheum. 23, 881
Targoff, I.N. (1990) Rheum. Dis. Clin. North Am. 18, 455
Mathews, M.B., & Bernstein, R.M. (1983) Nature 304, 177 Mirande, M. (1991) Prog. Nucl. Acid Res. 40, 95
Rosa, M.D. et al. (1983) Nucl. Acids Res. 11, 853
Biswas, T. et al. (1987) J. Immunol. Meth. 98, 235
Raben N. et al. (1991) Nucl. Acids Res. 20, 1075
Raben, N. et al. (1994) J. Biol. Chem. 269, 24277
Blechynden, L.M. et al. (1996) Gene 178, 151
Targoff, I.N., Reichlin, M. (1987) J. Immunol. 138, 2874
Walker, E.J. et al. (1987) J. Immunol. Meth. 96, 149