Z-domain of protein A scaffold protein anti-Human IgG
CAT#: SZA-L231
This IgG 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 for IgG 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
- IgG
- Species Reactivity
- Human
- Expression Host
- E. coli
- Applications
- ELISA; IHC; Microscopy; FC; WB; FuncS
Target
- Alternative Names
- Staphylococcal protein A; Z-domain of protein A; IgG; Immunoglobulin G
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Excellent for ELISA
I've been using the Z-domain of protein A scaffold protein in my laboratory for ELISA tests, and it's been a game-changer. The binding affinity and specificity for human IgG are excellent, and it has significantly improved our assay sensitivity.
Stable product
The stability of the Z-domain protein through various freeze-thaw cycles has made our workflow much more efficient. We've seen no degradation in performance, and it's reassuring to know that our reagents maintain their integrity over time.
Better specificity
The Z-domain of protein A has drastically improved the purity of our IgG extractions during immunoprecipitation. The high specificity reduces non-specific binding, which means cleaner samples and more reliable experimental outcomes.
Q&As
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What does it mean to use protein A scaffold protein's Z-domain for anti-Human IgG detection in research applications?
A: Protein A's Z-domain binds to the Fc region of human IgG antibodies with great affinity, which makes it an excellent tool for detecting, purifying, and quantifying IgGs in a variety of scientific and medical applications.
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Is there a difference between the binding ability of protein A scaffold protein's Z-domain and its full-length counterpart?
A: The Z-domain of protein A is engineered for optimal binding to human IgG, often providing comparable if not superior binding capacity to that of full-length protein A, particularly in certain applications where a smaller fragment is advantageous.
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What are some practical factors to take into account while conjugating a protein's Z-domain? An enzyme or fluorescent dye as a reporter molecule and a scaffold protein?
A: Important factors to consider include the preservation of binding activity after conjugation, optimal conjugation chemistry to avoid steric hindrance, and maintaining the integrity of the Z-domain to ensure effective IgG binding.
View the frequently asked questions answered by Creative Biolabs Support.
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