Secondary Antibodies

Anti-Guinea Pig IgG Antibody generated in donkey detects guinea pig 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-Guinea Pig IgG Fluorescein Antibody generated in donkey detects guinea pig 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

Anti-Guinea Pig IgG Peroxidase Antibody generated in donkey detects guinea pig 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

Anti-Guinea Pig IgG Alkaline Phosphatase Antibody generated in donkey detects guinea pig 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

Anti-Guinea Pig IgG Biotin Antibody generated in donkey detects guinea pig 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 comp

Anti-Guinea Pig IgG Texas Red Antibody generated in donkey detects guinea pig 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 c

Anti-Golden Syrian Hamster IgG Rhodamine Antibody generated in goat 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 host-species

Anti-Golden Syrian Hamster IgG Rhodamine Antibody generated in goat 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 host-species s

Anti-Golden Syrian Hamster IgG Antibody generated in goat 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 host-species source and