Secondary Antibodies

Anti-Rat IgM antibody specifically detects rat IgM heavy chain. Immunoglobulin M is the largest antibody isotype and the first to be secreted against an initial exposure to antigen. IgM is predominantly produced in the spleen. Formed from covalently linking 5 immunoglobulins together, the approximate molecular weight of IgM is 900kDa and possesses 10 binding sites (though due to the size of most antigens, not all sites are capable of binding at once). Due to this large size, IgM is typically isolated to the serum. Anti-Rat IgM antibody is ideal for investigators in Immunology, Microbiology, and Cell Biology. This Rat IgM Antibody is conjugated to rhodamine.

Anti-Rat IgG (H&L) generated in goat detects rat Immunoglobulin G. Both the Heavy and Light chains of the antibody molecule are present. Representing approximately 75% of serum immunoglobulins, IgG is the most abundant antibody isotype found in the circulation. IgG molecules are synthesized and secreted by plasma B cells. 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.

RAT IgG (H&L) (GOAT) Antibody was generated in goat detects specifically Rat IgG whole molecule. Anti-Rat IgG antibody is ideal for investigators involved in serum protein component research.

Rat IgM antibody recognizes the mu chain of the Rat IgM. No reaction was observed against Rat IgA or Rat IgG. ELISA was used to confirm specificity at less than 1% cross reactivity against other rat heavy or light chain isotypes. Anti-Rat IgM antibody is ideal with investigators involved in serum component protein research.

Anti-Rat IgG (H&L) Antibody Fluorescein Conjugated generated in goat detects reactivity to Rat 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 the 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-Rat IgG IgA IgM (H&L) Antibody generated in goat detects rat (heavy and light chain) immunoglobulin G, A, and M. Immunoglobulin G binds to antigens and can neutralize or opsonize targets, and are predominantly involved in the secondary immune response. Immunoglobulin A (IgA) is an antibody that plays a critical role in mucosal immunity. IgA has two subclasses (IgA1 and IgA2) and can exist in a dimeric form called secretory IgA (sIgA). Immunoglobulin M, or IgM, is a pentamer composed of 5 immunoglobulin molecules linked through their F(c) domain by the J chain. 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. This Anti-Rat IgG IgA IgM Antibody is conjugated to Fluorescein.

Anti-Rat IgG (H&L) rhodamine Antibody generated in goat detects reactivity to Rat 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 the 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 fr

Anti-Rat IgG whole molecule antibody generated in goat detects specifically Rat IgG whole molecule. This secondary antibody anti-Rat is ideal for investigators who routinely perform ELISA, Sandwich ELISA, titration assays, western-blot, immunoprecipitation and more generally immunoassays.

Rat IgG IgA IgM (H&L) Antibody detects immunoglobulin G, A, and M from Rat. Immunoglobulin G binds to antigens and can neutralize or opsonize targets, and are predominantly involved in the secondary immune response. Immunoglobulin A (IgA) is an antibody that plays a critical role in mucosal immunity. IgA has two subclasses (IgA1 and IgA2) and can exist in a dimeric form called secretory IgA (sIgA). Immunoglobulin M, or IgM, is a pentamer composed of 5 immunoglobulin molecules linked through their F(c) domain by the J chain.