The present disclosure pertains to compositions comprising anti-VEGF proteins.

The present invention relates to a chromatography ligand, which comprises Domain C from Staphylococcus protein A (SpA), or a functional fragment or variant thereof. The chromatography ligand presents an advantageous capability of withstanding harsh cleaning in place (CIF) conditions, and is capable of binding Fab fragments of antibodies. The ligand may be provided with a terminal coupling group, such as arginine or cysteine, to facilitate its coupling to an insoluble carrier such as beads or a membrane. The invention also relates process of using the ligand in isolation of antibodies, and to a purification protocol which may include washing steps and/or regeneration with alkali.

The present invention relates to a chromatography ligand, which comprises Domain C from Staphylococcus protein A (SpA), or a functional fragment or variant thereof. The chromatography ligand presents an advantageous capability of withstanding harsh cleaning in place (CIF) conditions, and is capable of binding Fab fragments of antibodies. The ligand may be provided with a terminal coupling group, such as arginine or cysteine, to facilitate its coupling to an insoluble carrier such as beads or a membrane. The invention also relates process of using the ligand in isolation of antibodies, and to a purification protocol which may include washing steps and/or regeneration with alkali.

An Fc-binding polypeptide of improved alkali stability, comprising a mutant of an 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:8, SEQ ID NO 26 or SEQ ID NO 27, wherein at least the alanine residue at the position corresponding to position 42 in SEQ ID NO:4-7 has been mutated to arginine and/or wherein at least the aspartic acid residue at the position corresponding to position 37 in SEQ ID NO:4-7 has been mutated to glutamic acid.

An Fc-binding polypeptide of improved alkali stability, comprising a mutant of an 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:8, SEQ ID NO 26 or SEQ ID NO 27, wherein at least the alanine residue at the position corresponding to position 42 in SEQ ID NO:4-7 has been mutated to arginine and/or wherein at least the aspartic acid residue at the position corresponding to position 37 in SEQ ID NO:4-7 has been mutated to glutamic acid.

A mixed mode affinity chromatography carrier includes a substrate, a hydrophilic polymer, an antibody-binding cyclic peptide, and a cation exchange group.

A mixed mode affinity chromatography carrier includes a substrate, a hydrophilic polymer, an antibody-binding cyclic peptide, and a cation exchange group.

Compositions and methods are described for self-assembled polymer materials having at least one of macro, meso, or micro pores.

Compositions and methods are described for self-assembled polymer materials having at least one of macro, meso, or micro pores.

A porous membrane obtainable by a process comprising curing a composition comprising: (i) cross-linking agent(s) comprising at least one ligand group; (ii) inert solvent(s); (iii) polymerization initiator(s); and (vi) optionally monomer(s) other than component (i) which are reactive with component (i); wherein the composition satisfies the following equation: Z=wt(i)/(wt(i)+wt(iii)+wt(iv)) wherein: Z has a value of at least 0.6; wt(i) is the number of grammes of component (i) present in the composition; wt(iii) is the number of grammes of component (iii) present in the composition; and wt(iv) is the number of grammes of component (iv) present in the composition.