Z-domain of protein A scaffold protein anti-Staphylococcus aureus Protein A Z domain
CAT#: SZA-L238
This protein A Z domain 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=6 μM) for protein A Z domain 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 Z domain
- Species Reactivity
- Staphylococcus aureus
- Expression Host
- E. coli
- Affinity Constant
- 6 μM
- Applications
- ELISA; IHC; Microscopy; FC; WB; FuncS
Target
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Scaffold Library Origins
We were interested in the engineering strategy behind this product. The fact that the primary scaffold was derived from a naive combinatorial library of the staphylococcal protein A Z domain provided a robust starting point for our binding assays.
Confirmed Binding Affinity
Our lab utilized biosensor technology to verify the specifications of this scaffold protein. We observed an affinity consistent with the reported KD of 6 μM, which was sufficient for our second-generation variant analysis in diagnostic development research.
Q&As
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How was the library for this scaffold protein constructed?
A: The primary scaffold protein was derived from a naive combinatorial library of the three-helix bundle Z domain of staphylococcal protein A. A hierarchical library was subsequently constructed through selective re-randomization of six amino acid positions in one of the alpha-helices.
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What is the binding affinity of this product?
A: Second-generation variants of this Z-domain scaffold were identified to have affinities (KD=6 μM) for the protein A Z domain. This value was determined using biosensor technology after selections involving monovalent phage display technology.
View the frequently asked questions answered by Creative Biolabs Support.
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