Recombinant Escherichia coli Elongation factor P (efp)

Category: Proteins
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CSB-EP358853ENV
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Product Name Recombinant Escherichia coli Elongation factor P (efp)
Description Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis.
Synonyms Short name:EF-P
Host E.coli
Molecular Weight 36.5
Amino Acid Sequence ATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK
Protein Length Full Length, 2-188aa
Tag N-terminal 6xHis-SUMO-tagged
Reactivity E.coli
Applications SDS-PAGE
Form Liquid, in Tris-based buffer, 50% glycerol
Purity Greater than 90% as determined by SDS-PAGE.
References "Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis."Aoki H., Adams S.-L., Chung D.-G., Yaguchi M., Chuang S.-E., Ganoza M.C.Nucleic Acids Res. 19:6215-6220(1991)
Background Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis.
Supplier Cusabio

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