Secondary Antibodies

Rabbit Anti-VhH antibody can be used to detect single domain VhH antibodies. The single-domain antibody (sdAb) is a small (12 - 14 kDa) antibody fragment that consists of a monomeric variable domain derived from the heavy chain, also called a VhH antibody. These heavy chain only Fab-like domains have activity that is similar to a whole antibody, and they are able to bind to a specific antigens. SdAb's are derived from camelid species that include llamas, alpacas and camels. Camelids produce both classical (containing heavy and light chain fragments) and non-classical antibody structures (containing only a heavy chain). VhH antibodies are the smallest functional antigen-binding fragment that occurs in nature and these are now being used in biotechnology as a novel antibody scaffold. The small size of the VhH single domain antibody makes it very attractive for use in diagnostic imaging and they have potential for therapeutic activity.

Rabbit Anti-VhH antibody can be used to detect single domain VhH antibodies. The single-domain antibody (sdAb) is a small (12 - 14 kDa) antibody fragment that consists of a monomeric variable domain derived from the heavy chain, also called a VhH antibody. These heavy chain only Fab-like domains have activity that is similar to a whole antibody, and they are able to bind to a specific antigens. SdAb's are derived from camelid species that include llamas, alpacas and camels. Camelids produce both classical (containing heavy and light chain fragments) and non-classical antibody structures (containing only a heavy chain). VhH antibodies are the smallest functional antigen-binding fragment that occurs in nature and these are now being used in biotechnology as a novel antibody scaffold. The small size of the VhH single domain antibody makes it very attractive for use in diagnostic imaging and they have potential for therapeutic activity.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region.

Immunoglobulin M is the largest antibody isotype and the first to be secreted against an initial exposure to antigen. IgM is predominantly produced in the spleen. Formed from covalently linking 5 immunoglobulins together, the approximate molecular weight of IgM is 900kDa and possesses 10 binding sites (though due to the size of most antigens, not all sites are capable of binding at once). Due to this large size, IgM is typically isolated to the serum. Anti-Bovine IgM antibody is ideal for investigators in Immunology, Microbiology, and Cell Biology.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. Secondary Antibodies are available in a variety of formats and conjugate types. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition. Anti-Cat IgG (H&L) antibody is ideal for investigators in Immunology, Cancer, and Microbiology research.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. Secondary Antibodies are available in a variety of formats and conjugate types. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition. Anti-Cat IgG F(ab')2 antibody is ideal for investigators in Immunology, Cancer, and Microbiology research.