Abstract: A multivalent antibody fusion protein comprising: a heavy chain comprising, in sequence from the N-terminal, a variable domain nominally VH1, a CH1 region and a further variable domain nominally VH2, a light chain comprising, in sequence from the N-terminal, a variable domain nominally VL1, a CL domain and a variable domain nominally VL2, wherein said heavy and light chains are aligned to provide a first binding site formed by a first variable domain pair of VH1 and VL1 and a second binding site formed by a second variable domain pair of VH2 and VL2, wherein there is a disulfide bond between a variable domain pair forming a binding site, and said fusion protein is conjugated to a PEG polymer.

Abstract: The present invention provides a recombinant gram-negative bacterial cell comprising a mutant spr gene encoding a mutant spr protein and wherein the cell comprises a non-recombinant wild-type chromosomal Tsp gene.

Abstract: The present invention provides a recombinant gram-negative bacterial cell comprising a mutant spr gene encoding a spr protein having a mutation at one or more amino acids selected from D133, H145, H157, N31, R62, I70, Q73, C94, S95, V98, Q99, R100, L108, Y115, V135, L136, G140, R144 and G147 and wherein the cell has reduced Tsp protein activity compared to a wild-type cell.

Abstract: The present invention provides a recombinant gram-negative bacterial cell, characterized in that the cell comprises a recombinant polynucleotide encoding DsbC and has reduced Tsp protein activity compared to a wild-type cell.

Abstract: The present invention provides a multivalent antibody or a heavy/light chain component thereof comprising: a heavy chain comprising a constant region fragment, said constant region fragment located between two variable domains which are not a cognate pair, the heavy chain further comprising an Fc region with at least one domain selected from CH2, CH3 and combinations thereof, with the proviso that the heavy chain contains no more than one CH1 domain and only contains two variable domains, and a light chain comprising a constant region fragment located between two variable domains which are not a cognate pair, wherein said heavy and light chains are aligned to provide a first binding site formed by a first cognate pair of variable domains and a second binding site formed by a second cognate pair of variable domains.

Abstract: A recombinant gram-negative bacterial cell comprising one or more of the following mutated protease genes: a) a mutated Tsp gene, wherein the mutated Tsp gene encodes a Tsp protein having reduced protease activity or is a knockout mutated Tsp gene; b) a mutated ptr gene, wherein the mutated ptr gene encodes a Protease III protein having reduced protease activity or is a knockout mutated ptr gene; and c) a mutated DegP gene encoding a DegP protein having chaperone activity and reduced protease activity; wherein the cell is isogenic to a wild-type bacterial cell except for the mutated Tsp gene and/or mutated ptr gene and/or mutated DegP gene and optionally a polynucleotide sequence encoding a protein of interest.

Abstract: The present invention provides a dicistronic message for producing an antibody molecule, in which the upstream cistron contains DNA coding for the light chain of the antibody and the downstream cistron contains DNA coding for the corresponding heavy chain, characterised in that the dicistronic message comprises a sequence selected from AEOS1 (SEQ ID NO:1), AEOS2 (SEQ ID NO:2), AEOS3 (SEQ ID NO:3), AEOS4 (SEQ ID NO: 4), AEOS5 (SEQ ID NO:5), AEOS6 (SEQ ID NO:6), AEOS7 (SEQ ID NO:7), AEOS8 (SEQ ID NO:8), AEOS9 (SEQ ID NO:9), AEOS1O (SEQ ID NO:10) and AEOS11 (SEQ ID NO:11).

Abstract: The present invention relates to a new class of modified antibody fragments. The present invention provides an antibody fragment to which one or more effector molecules is attached characterized in that the native interchain disulphide bond between the heavy (CHI) and light (CL) chain constant regions is absent and the heavy chain (CHI) and light chain (CL) constant regions are linked by an interchain disulphide bond between a pair of engineered cysteines, one in the light chain constant (CL) region and the other in the heavy chain constant (CHI) region.

Abstract: The present invention provides antibody Fab fragments in which the heavy chain constant region terminates at the interchain cysteine of CH1. Also provided are antibody Fab fragments in which the heavy chain constant region terminates at the interchain cysteine of CH1 to which one or more effector molecules are attached.

Abstract: The present invention provides an E. coli host cell expressing a recombinant antibody characterized in that the E. coli host cell has been genetically modified in order to change at least one physical property of one or more E. coli proteins which in the wild type co-purify with said recombinant antibody.

Abstract: The present invention provides dual specificity antibody fusion proteins comprising an antibody Fab or Fab? fragment with specificity for an antigen of interest, said fragment being fused to at least one single domain antibody which has specificity for a second antigen of interest.

Abstract: This invention relates to engineering of antibodies and more specifically provides altered antibodies of the IgG class to which one or more effector molecules are attached. The invention further relates to methods for the production of such conjugated antibodies.

Abstract: The present invention provides an Ecoli host cell expressing a recombinant antibody characterized in that the Ecoli host cell has been genetically modified in order to change at least one physical property of one or more Ecoli proteins which in the wild type copurify with said recombinant antibody.

Abstract: The present invention provides a dicistronic message for producing an antibody molecule, in which the upstream cistron contains DNA coding for the light chain of the antibody and the downstream cistron contains DNA coding for the corresponding heavy chain, characterised in that the dicistronic message comprises a sequence selected from AEOS1 (SEQ ID NO:1), AEOS2 (SEQ ID NO:2), AEOS3 (SEQ ID NO:3), AEOS4 (SEQ ID NO: 4), AEOS5 (SEQ ID NO:5), AEOS6 (SEQ ID NO:6), AEOS7 (SEQ ID NO:7), AEOS8 (SEQ ID NO:8), AEOS9 (SEQ ID NO:9), AEOS1O (SEQ ID NO:10) and AEOS1 1 (SEQ ID NO:11).

Abstract: The present invention relates to a new class of modified antibody fragments. The present invention provides an antibody fragment to which one or more effector molecules is attached characterized in that the native interchain disulphide bond between the heavy (CHI) and light (CL) chain constant regions is absent and the heavy chain (CHI) and light chain (CL) constant regions are linked by an interchain disulphide bond between a pair of engineered cysteines, one in the light chain constant (CL) region and the other in the heavy chain constant (CHI) region.

Abstract: Expression vectors encoding bacteriophage signal peptides are described. The vectors may be used for the heterologous expression and secretion of polypeptides such as antibodies in bacterial host cells.

Abstract: Expression vectors encoding bacteriophage signal peptides are described. The vectors may be used for the heterologous expression and secretion of polypeptides such as antibodies in bacterial host cells.

Abstract: Peptides comprising the amino acid sequence set forth in SEQ ID NO:1 are described wherein the amino acid at position 7 of SEQ ID NO:1 and the amino acid at position 8 of SEQ ID NO:1, which may be the same or different, is each a neutral aliphatic L-ammo acid residue, and protected and reactive derivatives thereof. The peptides may be used as hinge regions in proteins, wherein they are capable of being covalently coupled to achieve dimeric structures, for example, as found in antibodies.