Secondary Antibodies

Anti-Dog IgM antibody specifically detects dog IgM. 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-Dog 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-Dog IgG F(ab’)2 antibody is ideal for investigators in Immunology, Cancer, and Microbiology research.

Anti-Dog IgM antibody specifically detects dog IgM. 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-Dog IgM antibody is ideal for investigators in Immunology, Microbiology, and Cell Biology.

Anti-Goat IgG Fluorescein Antibody generated in mice detects goat IgG. 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. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both heavy and light chains of the antibody molecule are present.

Anti-Goat IgG Antibody generated in rabbit detects goat IgG. 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. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both heavy and light chains of the antibody molecule are present.

Anti-Goat IgG F(c) generated in rabbit is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme papain under controlled conditions of temperature, time and pH. Receptors bind the Fc portion of goat IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity.

Anti-Goat IgG F(ab')2 Antibody generated in rabbit is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. F(ab')2 molecules lack the Fc portion of IgG and therefore receptors that bind goat IgG F(c) will not bind goat IgG F(ab')2 molecules.

Anti-Goat IgM antibody specifically detects goat IgM. 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-Goat IgM antibody is ideal for investigators in Immunology, Microbiology, and Cell Biology.

Anti-Goat IgG [H&L] (Rabbit) Antibody Agarose Conjugated is generated in goat and detects specifically Goat IgG heavy and light chains. This anti-Goat antibody is suited for immobilization in a packed column for removal of Goat IgG from solution. Immunoglobulin G is the most abundant antibody isotype found in the circulation. IgG molecules are synthesized and secreted by plasma B cells. IgG antibodies are large molecules of about 150 kDa composed of four peptide chains. It contains two identical class gamma heavy chains of about 50 kDa and two identical light chains of about 25 kDa, thus a tetrameric quaternary structure. Anti-Goat IgG [H&L] Antibody is ideal for investigators in Cancer, Immunology, and Microbiology research.