Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

Abstract: A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an example DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin of Camelidae and is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the genera Aspergillus or Trichoderma, or a yeast, preferably belonging to the yeast genera Saccharomyces, Kluyveromyces, Hansenula, or Pichia. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody ex Camelidae can be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised in Camelidae against transition state molecules.

Abstract: There are provided methods for screening a library of VHH polypeptides for VHH polypeptides that bind to an antigen including subjecting a library of VHH polypeptides to antigen-affinity selection with the antigen.

Abstract: The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is derived from a so-called heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding one or several antigens and which is further naturally devoid of light chains, wherein the immunoglobulin having determined antigen specificity is devoid of CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

Abstract: The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is obtainable from a camelid heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding an antigen and which is further devoid of polypeptide light chains, wherein the immunoglobulin having determined antigen specificity is devoid of a CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

Abstract: The present invention relates to fragments, especially variable fragments of immunoglobulins which are by nature devoid of light chains, these fragments being nevertheless capable of exhibiting a recognition and binding activity toward specific antigens. The present invention further relates to the use of such immunoglobulin fragments formed of at least one heavy chain variable fragment or derived therefrom, for therapeutic or veterinary purposes and especially for passive immunotherapy or serotherapy.

Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

Abstract: The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is derived from a so-called heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding one or several antigens and which is further naturally devoid of light chains, wherein the immunoglobulin having determined antigen specificity is devoid of CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

Abstract: The present invention relates to fragments, especially variable fragments of immunoglobulins which are by nature devoid of light chains, these fragments being nevertheless capable of exhibiting a recognition and binding activity toward specific antigens. The present invention further relates to the use of such immunoglobulin fragments formed of at least one heavy chain variable fragment or derived therefrom, for therapeutic or veterinary purposes and especially for passive immunotherapy or serotherapy.

Abstract: The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is derived from a so-called heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding one or several antigens and which is further naturally devoid of light chains, wherein the immunoglobulin having determined antigen specificity is devoid of CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

Abstract: The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is derived from a so-called heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding one or several antigens and which is further naturally devoid of light chains, wherein the immunoglobulin having determined antigen specificity is devoid of CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

Abstract: A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an example DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin of Camelidae and is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the genera Aspergillus or Trichoderma, or a yeast, preferably belonging to the yeast genera Saccharomyces, Kluyveromyces, Hansenula, or Pichia. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody ex Camelidae can be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised in Camelidae against transition state molecules.

Abstract: A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an expressible DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin of Camelidae and is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the genera Aspergillus or Trichoderma, or a yeast, preferably belonging to the yeast genera Saccharomyces, Kluyveromyces, Hansenula, or Pichia. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody ex Camelidae can be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised in Camelidae against transition state molecules.

Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

Abstract: The present invention relates to fragments, especially variable fragments of immunoglobulins which are by nature devoid of light chains, these fragments being nevertheless capable of exhibiting a recognition and binding activity toward specific antigens. The present invention further relates to the use of such immunoglobulin fragments formed of at least one heavy chain variable fragment or derived therefrom, for therapeutic or veterinary purposes and especially for passive immunotherapy or serotherapy.

Abstract: A recombinant vector for cloning a heterologous nucleotide sequence and/or expressing it and/or transferring it to a cell host. The vector includes, at a site which is not essential for replication, the gene coding for a lipoprotein other than E. coli lipoproteins, or a part of said gene which contains the elements required for controlling the expression of said lipoprotein and exposing it on the surface of the outer host cell membrane, so that the heterologous nucleotide sequence can be inserted into the gene or said part thereof under conditions suitable for expressing said heterologous sequence and exposing it on the surface of the cell host.

Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

Abstract: There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.