Secondary Antibodies

Anti-Golden Syrian Hamster IgG Alkaline Phosphatase Antibody generated in rabbit detects Golden Syrian Hamster 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. 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 h

Anti-Golden Syrian Hamster IgG F(ab')2 Alkaline Phosphatase 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 Golden Syrian Hamster IgG F(c) will not bind Golden Syrian Hamster IgG F(ab')2 molecules. 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-Golden Syrian Hamster IgG F(ab')2 Biotin 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 Golden Syrian Hamster IgG F(c) will not bind Golden Syrian Hamster IgG F(ab')2 molecules. 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-Golden Syrian Hamster IgG F(ab')2 Texas Red 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 Golden Syrian Hamster IgG F(c) will not bind Golden Syrian Hamster IgG F(ab')2 molecules. 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-Horse IgG Rhodamine Antibody generated in goat detects horse 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. 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-Horse IgG F(c) generated in goat 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 horse IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity.

Anti-Horse IgG F(ab')2 Rhodamine Antibody generated in goat 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 horse IgG F(c) will not bind horse IgG F(ab')2 molecules. 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-Horse IgG Antibody generated in goat detects horse 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. 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.

Horse IgG F(c) antibody generated in goat recognizes the F(c) portion of horse IgG. 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 horse IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity. Anti-Horse IgG F(c) antibody is ideal for investigators involved in serum component protein research.