1. Preparation of an antibody recognizing both human and rodent MRP1.
- Author
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Fernetti C, Pascolo L, Podda E, Gennaro R, Stebel M, and Tiribelli C
- Subjects
- Amino Acid Sequence, Animals, Antibodies, Monoclonal immunology, Blotting, Western, Conserved Sequence, Epitopes chemistry, Epitopes immunology, Humans, Immune Sera biosynthesis, Immune Sera immunology, Immune Sera isolation & purification, Male, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Molecular Weight, Multidrug Resistance-Associated Protein 2, Multidrug Resistance-Associated Proteins chemistry, Peptides chemical synthesis, Peptides chemistry, Peptides immunology, Rats, Rats, Wistar, Sequence Alignment, Antibodies immunology, Antibodies isolation & purification, Antibody Specificity, Cross Reactions immunology, Membrane Transport Proteins, Multidrug Resistance-Associated Proteins immunology, Rodentia immunology
- Abstract
Based on the high level of identity among human, mouse, and rat MRP1 protein sequence, we produced a specific polyclonal antibody (MRP1-A23) against a synthetic polypeptide covering the C-terminus of the human protein. Western blot analysis showed a reactivity against human MRP1 similar to that obtained with the monoclonal QCRL1 antibody. Differently from other available antibodies against human MPR1, MRP1-A23 also detected both rat and mouse MRP1. No cross-reactivity was observed with either human or mouse MRP2 while MRP1-A23 weakly cross-reacted with rat MRP2 in the protein region ranging from 1512 to 1533 amino acids. These data indicate that MRP1-A23 allows specific MRP1 detection in both human and rodent tissues and may provide an important tool in the study of MRP1 expression and function in both experimental and clinical materials., (Copyright 2001 Academic Press.)
- Published
- 2001
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