An Fc-binding polypeptide of improved alkali stability, comprising a mutant of a parental Fc-binding domain of Staphylococcus Protein A (SpA), as defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO:3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:22, SEQ ID NO 51 or SEQ ID NO 52, wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO: 4-7 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.

An Fc-binding polypeptide of improved alkali stability, comprising a mutant of a parental Fc-binding domain of Staphylococcus Protein A (SpA), as defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO:3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:22, SEQ ID NO 51 or SEQ ID NO 52, wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO: 4-7 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.

The instant disclosure provides cellularized hydrogels containing cells encapsulated in linked polymers of hyaluronic acid, heparin and other components as described herein. Such cellularized hydrogels find use in variety of purposes including effective transplantation of cells into a host organism for cell therapy and the derivation of desired cell types. Other purposes include but are not limited to use as a tissue model for the in vitro study of cellular responses and behaviors. The instant disclosure also provides methods, including methods of making and using the described cellularized hydrogels. Also provided are kits that include components for making and/or using cellularized hydrogels e.g., according to the methods as described herein.

A first immunoglobulin chain variable region-binding peptide includes an amino acid sequence of SEQ ID NO: 20 with at least one substitution at one or more positions selected from the group consisting of the 41.sup.st position and the 42.sup.nd position. A second immunoglobulin chain variable region-binding peptide includes the amino acid sequence further comprising 1 to 20 amino acid deletions, substitutions and/or additions at one or more positions except for the 41.sup.st position and the 42.sup.nd position. A third immunoglobulin chain variable region-binding peptide includes an amino acid sequence having a sequence identity of 80% or more with the amino acid sequence of the first peptide, provided that the at least one substitution is not further mutated. The second and third peptides have a higher chemical stability to an alkaline aqueous solution than the chemical stability of the first peptide before introducing the substitution.

The invention relates to a separation matrix comprising at least 11 mg/ml Fc-binding ligands covalently coupled to a porous support, wherein: a) the ligands comprise multimers of alkali-stabilized Protein A domains, and b) the porous support comprises cross-linked polymer particles having a volume-weighted median diameter (d50,v) of 56-70 micrometers and a dry solids weight of 55-80 mg/ml.

The present disclosure provides antibodies specific for an epitope present on CD22. The antibodies are useful in various treatment, diagnostic, and monitoring applications, which are also provided.

The present disclosure provides antibodies specific for an epitope present on CD22. The antibodies are useful in various treatment, diagnostic, and monitoring applications, which are also provided.

The present invention concerns the preparation of solutions, particularly for implementing analytical methods, in particular by spectrometry, particularly for producing standard solutions which are useful, for example, for calibrating spectrometers or for implementing diagnostic methods. It allows the implementation of an easy process for preparing such standard solutions.

The present invention concerns the preparation of solutions, particularly for implementing analytical methods, in particular by spectrometry, particularly for producing standard solutions which are useful, for example, for calibrating spectrometers or for implementing diagnostic methods. It allows the implementation of an easy process for preparing such standard solutions.

An Fc-binding polypeptide of improved alkali stability, comprising a mutant of a parental Fc-binding domain of Staphylococcus Protein A (SpA), as defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 22, SEQ ID NO: 51 or SEQ ID NO: 52, wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO: 4-7 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.