The present invention generally relates to antibodies or binding fragments thereof capable of binding an allergen, in particular a food allergen as well as pharmaceutical compositions comprising such antibodies or binding fragments thereof for the treatment of allergy, in particular food allergy. In addition the invention relates to methods for evaluating the capacity of a candidate antibody or binding fragment thereof to inhibit allergen binding/and/or allergen- induced activity in a human and methods of detecting or quantifying whether an allergen is present in a sample.

The present invention generally relates to antibodies or binding fragments thereof capable of binding an allergen, in particular a food allergen as well as pharmaceutical compositions comprising such antibodies or binding fragments thereof for the treatment of allergy, in particular food allergy. In addition the invention relates to methods for evaluating the capacity of a candidate antibody or binding fragment thereof to inhibit allergen binding/and/or allergen- induced activity in a human and methods of detecting or quantifying whether an allergen is present in a sample.

Herein is reported a conjugate comprising an antigen and an antibody that specifically binds to the antigen wherein a covalent bond is formed between the antigen and an amino acid residue in the CDR2 of the antibody, an antibody comprising a cysteine residue at amino acid position 53 (according to Kabat) in the heavy chain CDR2 and uses thereof.

Herein is reported a conjugate comprising an antigen and an antibody that specifically binds to the antigen wherein a covalent bond is formed between the antigen and an amino acid residue in the CDR2 of the antibody, an antibody comprising a cysteine residue at amino acid position 53 (according to Kabat) in the heavy chain CDR2 and uses thereof.

A single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of -synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

A single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of -synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

The present invention provides anti-gliadin antibodies and antibody fragments, and polypeptides encoding the antibodies or fragment. Also disclosed are methods and Kits for the use of such antibodies, fragments, or polypeptides in detection of gliadin. Further provided are heavy chain and light chain variable sequences and associated sequences of complementarity-determining regions (CDRs).

The present invention provides anti-gliadin antibodies and antibody fragments, and polypeptides encoding the antibodies or fragment. Also disclosed are methods and Kits for the use of such antibodies, fragments, or polypeptides in detection of gliadin. Further provided are heavy chain and light chain variable sequences and associated sequences of complementarity-determining regions (CDRs).

A nucleic acid encodes a single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of -synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

A nucleic acid encodes a single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of -synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.