Jackson Immunoresearch

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...

Gamma globulins are purified from non-immunized animal serums by salt fractionation, ion-exchange chromatography and gel filtration. Gamma globulins are an inexpensive source of IgG with only trace amounts of other immunoglobulins and/or non-immunoglobulin serum proteins. Gamma globulins are...

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...

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...

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...

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...

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...

Steptavidin, a bacterial protein isolated from Streptomyces avidinii, is similar to egg-white avidin in its ability to bind biotin, and has been used as a replacement for egg-white avidin because of its more favorable chemical properties. Conjugates of streptavidin are recommended for use with...

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...

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...

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...

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...

ChromPure is our trade name for highly purified proteins from the serum of non-immunized animals. Host: Rabbit Product: IgG, whole molecule Conjugate: Unconjugated

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...