20240018184. Method of Cleaning and/or Sanitizing a Separation Matrix simplified abstract (CYTIVA BIOPROCESS R&D AB)
Contents
Method of Cleaning and/or Sanitizing a Separation Matrix
Organization Name
Inventor(s)
Gustav José Rodrigo of Uppsala (SE)
Tomas Bjorkman of Uppsala (SE)
Jesper Ulf Hansson of Uppsala (SE)
Method of Cleaning and/or Sanitizing a Separation Matrix - A simplified explanation of the abstract
This abstract first appeared for US patent application 20240018184 titled 'Method of Cleaning and/or Sanitizing a Separation Matrix
Simplified Explanation
The alkali-stabilized protein A domains are mutants of a parental Fc-binding domain of protein A (SPA). These mutants have specific amino acid changes at positions 13, 44, and 3 of the parental sequence.
- The amino acid residues at positions 13 and 44 of the parental sequence are asparagines.
- The asparagine residue at position 3 of the parental sequence has been mutated to an amino acid selected from a group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine, and arginine.
Potential applications of this technology:
- Enhanced stability of protein A domains: The alkali-stabilized mutants have improved stability, making them suitable for various biotechnological applications.
- Improved protein purification: The alkali-stabilized mutants can be used in affinity chromatography to efficiently purify target proteins.
- Antibody production: The mutants can be used in antibody production processes to enhance the binding and purification of antibodies.
Problems solved by this technology:
- Protein instability: The alkali-stabilized mutants address the issue of protein instability, which can affect the functionality and shelf-life of proteins.
- Inefficient protein purification: The mutants improve the efficiency of protein purification processes by enhancing the binding affinity between the target protein and protein A domains.
Benefits of this technology:
- Enhanced protein stability: The alkali-stabilized mutants offer improved stability, allowing for better preservation and longer shelf-life of proteins.
- Increased purification efficiency: The mutants improve the efficiency of protein purification processes, resulting in higher yields and purity of target proteins.
- Versatile applications: The alkali-stabilized mutants can be used in various biotechnological applications, including protein purification, antibody production, and other protein-based research and development activities.
Original Abstract Submitted
the alkali-stabilized protein a domains comprise mutants of a parental fc-binding domain of protein a (spa), as defined by seq id no 51 or seq id no 52, wherein the amino acid residues at positions 13 and 44 of seq id no 51 or 52 are asparagines and wherein at least the asparagine residue at position 3 of seq id no 51 or 52 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.
