Results for Secondary Antibodies ( 4371 )
Mouse IgG TrueBlot® ULTRA is a unique Anti-Mouse IgG monoclonal secondary antibody. Mouse IgG TrueBlot® ULTRA enables detection of immunoblotted target protein bands, without hindrance by interfering immunoprecipitating immunoglobulin heavy and light chains. It is easy to generate publication-quality IP/Western blot data with Mouse IgG TrueBlot® ULTRA, simply substitute the conventional Anti-Mouse IgG blotting reagent with Mouse IgG TrueBlot® ULTRA and follow the prescribed protocol for sample preparation and immunoblotting. Mouse IgG TrueBlot® ULTRA is ideal for use in protocols involving immunoblotting of immunoprecipitated proteins. Mouse IgG TrueBlot® ULTRA preferentially detects the non-reduced form of mouse IgG (IgG1, IgG2a, IgG2b, IgG3) over the reduced, SDS-denatured form of IgG. When the immunoprecipitate is fully reduced immediately prior to SDS-gel electrophoresis, reactivity of Mouse IgG TrueBlot® ULTRA with the 55 kDa heavy chains and the 23 kDa light chains of the im
Mouse IgG TrueBlot® ULTRA is a unique anti-mouse IgG monoclonal secondary antibody. Mouse IgG TrueBlot® ULTRA enables detection of immunoblotted target protein bands, without hindrance by interfering immunoprecipitating immunoglobulin heavy and light chains. It is easy to generate publication-quality IP/Western blot data with Mouse IgG TrueBlot® ULTRA, simply substitute the conventional Anti-Mouse IgG blotting reagent with Mouse IgG TrueBlot® ULTRA and follow the prescribed protocol for sample preparation and immunoblotting. Mouse IgG TrueBlot® ULTRA is ideal for use in protocols involving immunoblotting of immunoprecipitated proteins. Mouse IgG TrueBlot® ULTRA preferentially detects the non-reduced form of mouse IgG (IgG1, IgG2a, IgG2b, IgG3) over the reduced, SDS-denatured form of IgG. When the immunoprecipitate is fully reduced immediately prior to SDS-gel electrophoresis, reactivity of Mouse IgG TrueBlot® ULTRA with the 55 kDa heavy chains and the 23 kDa light chains of the im
Mouse IgG TrueBlot® ULTRA is a unique Anti-Mouse IgG monoclonal secondary antibody. Mouse IgG TrueBlot® ULTRA enables detection of immunoblotted target protein bands, without hindrance by interfering immunoprecipitating immunoglobulin heavy and light chains. It is easy to generate publication-quality IP/Western blot data with Mouse IgG TrueBlot® ULTRA, simply substitute the conventional Anti-Mouse IgG blotting reagent with Mouse IgG TrueBlot® ULTRA and follow the prescribed protocol for sample preparation and immunoblotting. Mouse IgG TrueBlot® ULTRA is ideal for use in protocols involving immunoblotting of immunoprecipitated proteins. Mouse IgG TrueBlot® ULTRA preferentially detects the non-reduced form of mouse IgG (IgG1, IgG2a, IgG2b, IgG3) over the reduced, SDS-denatured form of IgG. When the immunoprecipitate is fully reduced immediately prior to SDS-gel electrophoresis, reactivity of Mouse IgG TrueBlot® ULTRA with the 55 kDa heavy chains and the 23 kDa light chains of the im
Rabbit Anti-VHH antibody can be used to detect single domain VHH antibodies. The single-domain antibody (sdAb) is a small (12 - 14 kDa) antibody fragment that consists of a monomeric variable domain derived from the heavy chain, also called a VHH antibody. These heavy chain only Fab-like domains have activity that is similar to a whole antibody, and they are able to bind to a specific antigens. SdAb's are derived from camelid species that include llamas, alpacas and camels. Camelids produce both classical (containing heavy and light chain fragments) and non-classical antibody structures (containing only a heavy chain). VHH antibodies are the smallest functional antigen-binding fragment that occurs in nature and these are now being used in biotechnology as a novel antibody scaffold. The small size of the VHH single domain antibody makes it very attractive for use in diagnostic imaging and they have potential for therapeutic activity.
Rabbit Anti-VHH antibody can be used to detect single domain VHH antibodies. The single-domain antibody (sdAb) is a small (12 - 14 kDa) antibody fragment that consists of a monomeric variable domain derived from the heavy chain, also called a VHH antibody. These heavy chain only Fab-like domains have activity that is similar to a whole antibody, and they are able to bind to a specific antigens. SdAb's are derived from camelid species that include llamas, alpacas and camels. Camelids produce both classical (containing heavy and light chain fragments) and non-classical antibody structures (containing only a heavy chain). VHH antibodies are the smallest functional antigen-binding fragment that occurs in nature and these are now being used in biotechnology as a novel antibody scaffold. The small size of the VHH single domain antibody makes it very attractive for use in diagnostic imaging and they have potential for therapeutic activity.
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(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.
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(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region.
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(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.