Overview
- Peptide (C)IQKENSREALVEPA, corresponding to residues 261-274 of rat NHERF-1 (Accession Q9JJ19). Between the PDZ2 and the ERM binding domains.
- Rat kidney membranes (1:200-1:500).
- Western blotting of rat kidney membranes:1. Anti-NHERF-1/EBP50 Antibody (APZ-006), (1:200).
2. Anti-NHERF-1/EBP50 Antibody, preincubated with NHERF-1/EBP50 Blocking Peptide (#BLP-PZ006).
The Na+/H+ exchange regulatory factor (EBP-50 or NHERF-1) is a 55 kD cytoplasmic protein adaptor that recruits a wide variety of cellular proteins.
Many of the interacting proteins do so through the two tandem PDZ domains (protein-binding domains conserved in the mammalian synaptic protein PSD-95/DlgA/ZO-1) and the C-terminal ERM (ezrin, radixin, moesin) binding region.
NHERF-1 was first identified as an adaptor necessary for the function of the Na+/H+ exchanger isoform 3 (NHE3) in renal apical cells.1 Since then it has been identified in cells of epithelial origin in several tissues such as gastrointestinal and lung.
NHERF-1 has been shown to interact with a growing number of proteins including ion channels (ROMK, CFTR, P2Y1, TRPC4 and TRPC6), growth factor receptors (PDGFR), phospholipase C isoforms (PLCb1, PLCb2, PLCb3), non-receptor protein tyrosine kinases (YAP65) and several cytoskeletal proteins that link membrane proteins to the underlying actin cytoskeleton.2
Recently, it has been shown that NHERF-1 expression was elevated in breast tumors compared to the expression in adjacent normal tissue.3