Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Wolfgang Northemann"'
Autor:
Todd A. Braciak, Wolfgang Northemann, Jack Gauldie, Masahira Hattori, Frank Lee, Lawrence J. Abraham, Marianne F. Reymond, G H Fey, Raymond G. Fletcher, Matthias Baumann
Publikováno v:
Annals of the New York Academy of Sciences. 557:317-331
Publikováno v:
Annals of the New York Academy of Sciences. 557:46-59
Publikováno v:
Annals of the New York Academy of Sciences. 557:536-539
Publikováno v:
Hybridoma. 15:103-108
Glutamate decarboxylase (GAD65) is a major autoantigen in insulin-dependent diabetes (IDDM) and the neurological disorder Stiff-Man-Syndrome (SMS). We derived a human monoclonal autoantibody (MICA 2) from peripheral blood of a patient newly diagnosed
Publikováno v:
Journal of Clinical Laboratory Analysis. 10:193-204
The extracellular domain of the TSH receptor (TSHR-561, amino acids #78-389) was expressed as a hexa-histidine fusion protein in bacteria. The recombinant protein was purified to homogeneity and used to immunize porcine and ovine species. High titre
Autor:
Nicholas Hunt, Michael Walter, Heike Berg, Wolfgang Northemann, Steve Fenning, Gisela Stahnke
Publikováno v:
Protein Expression and Purification. 6:748-756
Various nuclear proteins are the major targets of autoimmune responses in various rheumatic disorders. In particular, autoantibodies directed against a 68-kDa protein associated with the (U1) RNA-containing small nuclear ribonucleoprotein complexes t
Autor:
Werner A. Scherbaum, Wolfgang Northemann, Bernhard O. Boehm, Sabine Bieg, Ludwig Mauch, Jochen Seissler, Nadja Yassin
Publikováno v:
Autoimmunity. 19:231-238
By using an immunoprecipitation assay, we analysed reactivity of autoantibodies to human recombinant GAD65 and GAD67 in sera from patients with autoimmune polyendocrine syndrome Type II (APS II) with and without Type 1 (insulin-dependent) diabetes me
Publikováno v:
Journal of Clinical Laboratory Analysis. 8:163-166
The human insulin domains, signal peptide, B-chain, C-peptide, and A-chain, were highly expressed in Escherichia coli as recombinant proteins N-terminally fused to glutathione-S-transferase and a histidinehexapeptide. The recombinant proteins were pu
Publikováno v:
Journal of Immunological Methods. 164:221-231
A novel prokaryotic expression vector pGEX-6T was designed for high-level expression of recombinant fusion protein with a histidine-hexapeptide and glutathione-S-transferase at its N-terminus and the recombinant human preproinsulin at its C-terminus.