Z-domain of protein A scaffold protein anti-Human hRaf-1
CAT#: SZA-L225
This hRaf-1 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=1.9 μm) for hRaf-1 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
- hRaf-1
- Species Reactivity
- Human
- Expression Host
- BL21 (DE3) cells
- Affinity Constant
- 1.9 μm
- Applications
- ELISA; IHC; Microscopy; FC; WB; FuncS
Target
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