Expression of an EF-1 alpha-like rat cDNA, S1, in E. coli and production of a rabbit polyclonal antiserum to the recombinant protein.
A previously identified rat cDNA (S1) that shares 78% nucleotide homology and a predicted 92% amino acid homology with human EF-1 alpha was constructed into PGEX-2T and inducibly expressed in E. coli as a fusion protein. The purified recombinant S1 protein (rpS1) was used to raise rabbit antiserum which recognized rpS1 but not EF-1 alpha on immunoblots. A polyclonal antiserum to EF-1 alpha failed to react with the rpS1. Our results indicate that rpS1 protein can be used to produce antibodies which distinguish pS1 from EF-1 alpha despite their extensive amino acid sequence homology.
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Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Québec, Canada.
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Wang
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D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D000918:Antibody Specificity; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000096:biosynthesis* / Q000235:genetics* / Q000276:immunology*; D012333:RNA, Messenger / Q000235:genetics; D011817:Rabbits / Q000276:immunology; D051381:Rats / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D017386:Sequence Homology, Amino Acid
D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D012333:RNA, Messenger; D011993:Recombinant Fusion Proteins