Ankyrin repeat anti-α-Na,K-ATPase (SAR-L043)

The Ankyrin repeat that bound α-Na,K-ATPase was isolated from the library using Phage display techonology. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin repeats mediate protein–protein interactions and are among the most common structural motifs in known proteins. After affinity maturation, Ankyrin repeat variants were identified having affinities (KD=10-25 nM) for α-Na,K-ATPase as determined by biosensor technology. It's potential to be used in diagnostic, research and therapeutic applications.      

Scaffold Name
Ankyrin repeat
Ankyrin repeat proteins
Core Structure
2α-helices, β-turn
Variable Regions
b-turn,1a-helix and loop
Species Reactivity
Expression Host
BL21 (DE3) cells
Affinity Constant
10-25 nM
ELISA; immunohistochemistry; Microscopy; Flow Cytometer; Western Blotting; Functional Study
Alternative Names
Ankyrin repeat proteins; Ankyrin repeat; α-Na,K-ATPase; Na+/K+ pump; sodium-potassium pump

For lab research use only, not for diagnostic, therapeutic or any in vivo human use.

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