eRF1 Antibody recognizes endogenous levels of total eRF1 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe117 of human eRF1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
原厂资料:
Specificity / Sensitivity
eRF1 Antibody recognizes endogenous levels of total eRF1 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe117 of human eRF1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Efficient termination of mRNA translation in eukaryotes is dependent upon a complex of two polypeptide release factors, eRF1 and eRF3 (1). The eukaryotic translation termination factor 1 (eRF1, ETF1) structurally resembles tRNA, which allows it to participate in stop codon recognition as well as hydrolysis of the peptidyl-tRNA conjugate (2,3). The eRF1 protein contains three functionally distinct domains, including an amino-terminal domain that harbors discrete motifs that participate in stop codon recognition (4,5). Lysine hydroxylation within the amino-terminal domain is required for efficient termination of mRNA translation (6). The central region of eRF1 harbors a GGQ motif that facilitates hydrolysis of peptidyl-tRNA conjugates (7), while its carboxy terminus participates in eRF3 binding (8).