Secondary Antibodies

Anti-Chicken IgG F(c) Antibody detects specifically Chicken IgY F(c). It 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 chicken IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity. Anti-Chicken IgG F(c) Antibody is ideal for investigators in Cancer, Immunology, and Microbiology research.

Anti-Chicken 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 Chicken IgG F(c) will not bind Chicken IgG F(ab')2 molecules.

Anti-Chicken IgG Fluorescein Antibody generated in rabbit detects chicken IgY. 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-Chicken IgG F(c) Antibody detects specifically Chicken IgG F(c). It 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 chicken IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity. Anti-Chicken IgG F(c) Antibody is ideal for investigators in Cancer, Immunology, and Microbiology research.

Anti-Chicken 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 Chicken IgG F(c) will not bind Chicken IgG F(ab')2 molecules.

Anti-Chicken IgG Peroxidase Antibody generated in rabbit detects chicken IgY. 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-Chicken IgG F(c) Antibody detects specifically Chicken IgG F(c). It 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 chicken IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity. Anti-Chicken IgG F(c) Antibody is ideal for investigators in Cancer, Immunology, and Microbiology research.

Anti-Chicken 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 Chicken IgG F(c) will not bind Chicken IgG F(ab')2 molecules.

Anti-Chicken IgG Biotin Antibody generated in rabbit detects chicken IgY. 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.