Results for Secondary Antibodies ( 4372 )
TrueBlot® Magnetic Beads are uniform, non-aggregating, super-paramagnetic beads consisting of a ferric oxide core functionalized with various silane groups. The super-paramagnetic nanoparticles are coupled with a biomolecule, such as rabbit Anti-goat IgG, and are specifically designed, tested and quality controlled for isolation and purification of goat IgG, and immunoprecipitation methods using manual or automatic platforms. This antibody binds the heavy chain of goat IgG and is suitable for immunoassays that utilize a goat IgG primary polyclonal antibody. Cell separation and sorting can be achieved using a goat IgG antibody to defined cell surface antigens. The beads have a large surface area with high capture efficiencies. The beads are in suspension and will settle upon storage. Prior to use, mix the vial gently (do not vortex) to ensure delivery of proper bead volume. Bead mean diameter is ~0.5 μm, bead concentration is 5 mg/mL.
TrueBlot® Anti-Rabbit Ig IP Agarose Beads are a suspension of activated agarose beads coupled with goat Anti-rabbit IgG. It is suitable for precipitation of rabbit IgGs used as the primary antibodies in immunoprecipitation assays. The beads are in suspension and will settle upon storage. Prior to use, mix the vial gently (do not vortex) to ensure delivery of proper bead volume.
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(c) region, recognized by high-affinity Fc receptor proteins.
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(c) region, recognized by high-affinity Fc receptor proteins.
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(c) region, recognized by high-affinity Fc receptor proteins.
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(c) region, recognized by high-affinity Fc receptor proteins.
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(c) region, recognized by high-affinity Fc receptor proteins.
Anti-Chicken IgG Rhodamine 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 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.