Literature DB >> 2957274

Detection of heterologous fusion proteins in Escherichia coli with a monoclonal antibody.

M Zweig, S D Showalter, G C Du Bois, W P Sisk, D L Court.   

Abstract

Several laboratories have constructed expression vectors for the production of heterologous fusion proteins containing the N-terminal 13 amino acids of the bacteriophage lambda cII-coded protein in Escherichia coli. We have prepared a monoclonal antibody to a synthetic peptide having this CII amino acid sequence and have found that this antibody reacts with authentic CII protein in Western blot tests and with most CII peptide-containing fusion proteins in both radioimmunoprecipitation and Western blot assays. However, there are some CII-hybrid protein species with which the antibody does not react. Our findings indicate that this antibody is a valuable tool for detecting and purifying expressed proteins and in studying their structure and function.

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Year:  1987        PMID: 2957274     DOI: 10.1016/0378-1119(87)90247-2

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  2 in total

1.  Functional organization of the murine leukemia virus reverse transcriptase: characterization of a bacterially expressed AKR DNA polymerase deficient in RNase H activity.

Authors:  J G Levin; R J Crouch; K Post; S C Hu; D McKelvin; M Zweig; D L Court; B I Gerwin
Journal:  J Virol       Date:  1988-11       Impact factor: 5.103

2.  Expression in bacteria of functional inhibitory subunit of retinal rod cGMP phosphodiesterase.

Authors:  R L Brown; L Stryer
Journal:  Proc Natl Acad Sci U S A       Date:  1989-07       Impact factor: 11.205

  2 in total

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