Literature DB >> 2478393

Defined monoclonal antibodies to Escherichia coli beta-galactosidase as a tool for characterisation of recombinant expression products.

M Bröker1, H P Harthus.   

Abstract

Mouse monoclonal antibodies were prepared against beta-galactosidase (EC 3.2.1.23) of Escherichia coli. The binding sites of these monoclonal antibodies within the beta-galactosidase molecule were estimated by immunoblot analyses to various defined peptide regions of beta-galactosidase, encoded by expression plasmids. Monoclonal antibodies were characterised, which either bind to the amino-terminal or to the carboxy-terminal region or to an internal section of beta-galactosidase. These defined monoclonal antibodies were shown to be a useful tool for characterisation of beta-galactosidase fusion proteins expressed in Escherichia coli.

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Year:  1989        PMID: 2478393     DOI: 10.1016/0014-5793(89)81800-9

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Generation and application of a monoclonal antibody raised against a recombinant cytomegalovirus-specific polypeptide.

Authors:  G Jahn; H P Harthus; M Bröker; B Borisch; B Platzer; B Plachter
Journal:  Klin Wochenschr       Date:  1990-10-17

2.  Nuclear targeting of the tegument protein pp65 (UL83) of human cytomegalovirus: an unusual bipartite nuclear localization signal functions with other portions of the protein to mediate its efficient nuclear transport.

Authors:  S Schmolke; P Drescher; G Jahn; B Plachter
Journal:  J Virol       Date:  1995-02       Impact factor: 5.103

3.  Fine mapping of HIV-1 Nef-epitopes by monoclonal antibodies.

Authors:  H Siakkou; S Jahn; N Kienzle; R Ulrich; C Grötzinger; T Schneider; B Kohleisen; G Pauli; R Spohn; G Jung
Journal:  Arch Virol       Date:  1993       Impact factor: 2.574

  3 in total

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