Z-domain of protein A scaffold protein anti-Staphylococcus aureus Protein A
CAT#: SZA-L237
This protein A specific binding protein (Z-domain of protein A) was investigated by an α-helix shuffling strategy. The primary scaffold protein was from a naive combinatorial library of the three-helix bundle Z domain derived from staphylococcal protein A. A hierarchical library was constructed through selective re-randomization of six amino acid positions in one of the two α-helices of the domain, making up the Taq DNA polymerase binding surface. After selections using monovalent phage display technology, second generation variants were identified having affinities (KD=20 nM) for protein A as determined by biosensor technology. It's potential to be used in diagnostic, research and therapeutic applications.
Specifications
- Scaffold Name
- Z-domain of protein A
- Origin
- Staphylococcal protein A
- Core Structure
- 3-α helixes
- Variable Regions
- 13 Residues on first and second helix surface
- Target
- Protein A
- Species Reactivity
- Staphylococcus aureus
- Expression Host
- E. coli
- Affinity Constant
- 20 nM
- Applications
- ELISA; IHC; Microscopy; FC; WB; FuncS
Target
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Validated By Phage Display
Knowing this protein was selected using monovalent phage display technology gave us confidence in its specificity. Our ELISA results confirmed it binds the target successfully, validating the helix shuffling strategy employed during its development.
Impressive Affinity Maturation
The hierarchical library construction used to create this variant evidently paid off. We measured the affinity for Protein A and confirmed the KD was approximately 20 nM, which is significantly tighter than some first-generation scaffolds we have tested previously.
Q&As
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How does this variant differ in affinity from early generations?
A: Through the construction of a hierarchical library and selective re-randomization, second-generation variants were identified with significantly improved binding. Specifically, this product has an affinity (KD=20 nM) for protein A as determined by biosensor technology.
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What structural strategy was used to investigate this protein?
A: This protein A specific binding protein was investigated by an alpha-helix shuffling strategy. The primary scaffold is based on the three-helix bundle Z domain derived from staphylococcal protein A, with re-randomization of positions making up the Taq DNA polymerase binding surface.
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