Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Based on antigen-binding assay, Western blotting, and/or ELISA, the antibody reacts with the light chains on rabbit IgG and with those common to other rabbit immunoglobulins. The antibody does not react with the heavy chain of rabbit IgG. The antibody has been tested by ELISA to ensure minimal…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

F(ab')₂ fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')₂ fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they…

F(ab')₂ fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')₂ fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

F(ab')₂ fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')₂ fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

F(ab')2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')2 fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they are divalent. The…

F(ab')₂ fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')₂ fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

F(ab')2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')2 fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they are divalent. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

F(ab')2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')2 fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they are divalent. The…

F(ab')2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')2 fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they are divalent. The…

Fab fragment antibodies are generated by papain digestion of whole IgG antibodies to remove the entire Fc portion, including the hinge region. These antibodies are monovalent, containing only a single antigen binding site. The molecular weight of Fab fragments is about 50 kDa. Based on…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

F(ab')₂ fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region. F(ab')₂ fragments have two antigen-binding Fab portions linked together by disulfide bonds and therefore they…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The…