Abstract: There is provided method of profiling protein tyrosine phosphorylation of a sample, the method comprising: contacting the sample with an SH2 Superbinder in order to bind pTyr-including peptides contained in the sample with the SH2 Superbinder; isolating the bound pTyr-including peptides from the sample; and identifying the isolated pTyr-including peptides.

Abstract: There is provided method of profiling protein tyrosine phosphorylation of a sample, the method comprising: contacting the sample with an SH2 Superbinder in order to bind pTyr-including peptides contained in the sample with the SH2 Superbinder; isolating the bound pTyr-including peptides from the sample; and identifying the isolated pTyr-including peptides.

Abstract: The present invention relates to variant SH2 domains for binding a phosphotyrosine (pTyr)-containing peptide. The variant SH2 domains of the present invention include a parent SH2 domain having at least one amino acid substitution in a pre-defined region of 15 amino acid positions of the parent SR2 domain, wherein said at least one amino acid substitution increases the affinity of the variant SH2 domain for the pTyr-containing peptide relative to the parent SH2 domain. The present application relates also to methods of using the variant SH2 domains in the treatment of protein kinase-associated disorders, or the diagnosis or prognosis of protein kinase-associated disorders, for isolating and measuring the concentration of pTyr-containing molecules, and as reagents in research.

Abstract: The present invention relates to variant SH2 domains for binding a phosphotyrosine (pTyr)-containing peptide. The variant SH2 domains of the present invention include a parent SH2 domain having at least one amino acid substitution in a pre-defined region of 15 amino acid positions of the parent SR2 domain, wherein said at least one amino acid substitution increases the affinity of the variant SH2 domain for the pTyr-containing peptide relative to the parent SH2 domain. The present application relates also to methods of using the variant SH2 domains in the treatment of protein kinase-associated disorders, or the diagnosis or prognosis of protein kinase-associated disorders, for isolating and measuring the concentration of pTyr-containing molecules, and as reagents in research.

Abstract: The present invention relates to variant SH2 domains for binding a phosphotyrosine (pTyr)-containing peptide. The variant SH2 domains of the present invention include a parent SH2 domain having at least one amino acid substitution in a pre-defined region of 15 amino acid positions of the parent SR2 domain, wherein said at least one amino acid substitution increases the affinity of the variant SH2 domain for the pTyr-containing peptide relative to the parent SH2 domain. The present application relates also to methods of using the variant SH2 domains in the treatment of protein kinase-associated disorders, or the diagnosis or prognosis of protein kinase-associated disorders, for isolating and measuring the concentration of pTyr-containing molecules, and as reagents in research.

Abstract: The present invention relates to immunoglobulin (Ig)-binding proteins with alkali-resistance properties. In one embodiment, the present invention provides for a variant of an Ig-binding protein, the variant comprising the Ig-binding protein having at least one asparagine residue substituted with a histidine, a serine, an aspartic acid or a threonine residue. The at least one substitution may confer to the variant Ig-binding protein an increased stability in alkaline solutions when compared to the wild-type Ig-binding. The present invention relates also to matrices for affinity separation of immunoglobulins comprising the Ig-binding proteins of the present invention, and to methods of using the Ig-binding proteins of the present invention to separate immunoglobulins from mixture compositions.

Abstract: Provided are a support for affinity chromatography which has excellent alkali resistance, and a method for isolating immunoglobulin. A support for affinity chromatography, containing an immobilized protein ligand represented by the following formula (1): R—R2??(1) wherein R represents a polypeptide consisting of 4 to 30 amino acid residues that contains an amino acid sequence represented by ATK or ASK; and R2 represents a polypeptide consisting of 50 to 500 amino acid residues containing an immunoglobulin-binding domain consisting of an amino acid sequence represented by SEQ ID NO: 1 or SEQ ID NO: 2, the partial sequence thereof, or an amino acid sequence having 70% or more identity to these sequences; with the proviso that a terminus at which R2 binds to R is C-terminus or N-terminus of the immunoglobulin-binding domain.

Abstract: The present invention relates to immunoglobulin (Ig)-binding proteins with alkali-resistance properties. In one embodiment, the present invention provides for a variant of an Ig-binding protein, the variant comprising the Ig-binding protein having at least one asparagine residue substituted with a histidine, a serine, an aspartic acid or a threonine residue. The at least one substitution may confer to the variant Ig-binding protein an increased stability in alkaline solutions when compared to the wild-type Ig-binding. The present invention relates also to matrices for affinity separation of immunoglobulins comprising the Ig-binding proteins of the present invention, and to methods of using the Ig-binding proteins of the present invention to separate immunoglobulins from mixture compositions.

Abstract: Provided are a support for affinity chromatography which has excellent alkali resistance, and a method for isolating immunoglobulin. A support for affinity chromatography, containing an immobilized protein ligand represented by the following formula (1): R—R2??(1) wherein R represents a polypeptide consisting of 4 to 30 amino acid residues that contains an amino acid sequence represented by ATK or ASK; and R2 represents a polypeptide consisting of 50 to 500 amino acid residues containing an immunoglobulin-binding domain consisting of an amino acid sequence represented by SEQ ID NO: 1 or SEQ ID NO: 2, the partial sequence thereof, or an amino acid sequence having 70% or more identity to these sequences; with the proviso that a terminus at which R2 binds to R is C-terminus or N-terminus of the immunoglobulin-binding domain.