Secondary Antibodies

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 goat Anti-mouse IgG, and are specifically designed, tested and quality controlled for isolation and purification of mouse IgG, and immunoprecipitation methods using manual or automatic platforms. This antibody binds the heavy chain of mouse IgG and is suitable for immunoassays that utilize a mouse IgG primary polyclonal antibody. Cell separation and sorting can be achieved using a mouse 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® 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® 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.

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.