NHERF1 (Na+/H+ Exchanger Regulatory Factor,Na(+)/H(+) Exchange Regulatory Cofactor NHE-RF1,NHERF-1,NHERF,Ezrin-Radixin-Moesin Binding Phosphoprotein 50,EBP50,NPHLOP2,Regulatory Cofactor of Na(+)/H(+) Exchanger,Sodium-hyd

Antibodies / Antibodies-Ion Transport

-20°C

Supplied as a liquid in PBS, pH 7.4, 15mM sodium azide.

Bacterially produced recombinant full-length human NHERF.

EBP 50 [ERM (ezrin-radixin-moesin) binding phosphoprotein of 50kD] is a PDZ containing protein that is involved in the linkage of integral membrane proteins to the cytoskeleton. EBP50 contains two tandem PDZ domains followed by a carboxy-terminal sequence that binds to members of the ERM family of membrane-cytoskeleton adaptors. The PDZ domains within EBP50 bind to the carboxy termini of such target proteins as beta2 adrenergic receptor, platelet-derived growth factor receptor (PDGFR), and the cystic fibrosis conductance regulator (CFTR). The PDZ domains are also believed to be involved in the oligomerization of EBP 50 to form multiprotein complexes which helps to facilitate the formation of functional signalling complexes.

EBP 50 has been shown to link integral membrane proteins to the cytoskeleton by binding to members of the ERM family of proteins, which bind to F-actin. Through these interactions, EBP 50 is implicated in the localization of interactive groups of proteins into subcellular domains and in the regulation of activity of those interacting proteins. Immunohistochemical studies have shown that EBP 50 is found exclusively at the apical membranes of epithelial cells.

Applications:
Suitable for use in Immunoprecipitation and Western Blott. Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.