Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG3 but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule mouse IgG. It also reacts with the light chains of other mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, chicken, goat, guinea pig, syrian hamster, horse, human, rabbit, rat and sheep serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc portion of human IgG heavy chain but not with the Fab portion of human IgG. No antibody was detected against human IgM or IgA, or against non-immunoglobulin serum proteins. The antibody exhibits inherent minimal cross-reaction to mouse serum proteins and has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, horse and mouse serum proteins. The antibody may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule syrian hamster IgG. It also reacts with the light chains of other syrian hamster immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, horse, human, mouse, rabbit and rat serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule horse IgG. It also reacts with the light chains of other horse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc portion of human IgG heavy chain but not with the Fab portion of human IgG. No antibody was detected against human IgM or IgA, or against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, horse and mouse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule chicken IgY. It also reacts with the light chains of other chicken immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, goat, guinea pig, syrian hamster, horse, human, mouse, rabbit, rat and sheep serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc portion of mouse IgG heavy chain but not with the Fab portion of mouse immunoglobulins. No antibody was detected against mouse IgM or non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the heavy chain of mouse IgM but not with mouse IgG or the light chains of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with IgM from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG3 but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the heavy chain of mouse IgM but not with mouse IgG or the light chains of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with IgM from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule mouse IgG. It also reacts with the light chains of other mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine, horse, rabbit and rat serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule rat IgG. It also reacts with the light chains of other rat immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the F(ab')2 /Fab portion of rat IgG. It also reacts with the light chains of other rat immunoglobulins. No antibody was detected against the Fc portion of rat IgG or against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the F(ab')2 /Fab portion of rat IgG. It also reacts with the light chains of other rat immunoglobulins. No antibody was detected against the Fc portion of rat IgG or against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the F(ab')2 /Fab portion of mouse IgG. It also reacts with the light chains of other mouse immunoglobulins. No antibody was detected against the Fc portion of mouse IgG or against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG2a but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the heavy chain of mouse IgM but not with mouse IgG or the light chains of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with IgM from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the F(ab')2 /Fab portion of mouse IgG. It also reacts with the light chains of other mouse immunoglobulins. No antibody was detected against the Fc portion of mouse IgG or against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and horse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule mouse IgG. It also reacts with the light chains of other mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine, horse, rabbit and swine serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on anitgen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG2b but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG2c but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc portion of human IgG heavy chain but not with the Fab portion of human IgG. No antibody was detected against human IgM or IgA, or against non-immunoglobulin serum proteins. The antibody exhibits inherent minimal cross-reaction to mouse serum proteins and has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, horse and mouse serum proteins. The antibody may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with human lactoferrin in human milk. No antibody was detected against other human milk or serum proteins. The antibody may cross-react with lactoferrin from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the heavy chain of human IgA but not with human IgG or IgM. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with IgA from other species.

Supplier: Jackson Immunoresearch Lab

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 average molecular weight is about 110 kDa. They are used for specific applications, such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule human IgG. It also reacts with the light chains of other human immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the heavy chain of human IgA but not with human IgG or IgM. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with IgA from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule goat IgG. It also reacts with the light chains of other goat immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

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 form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule chicken IgY. It also reacts with the light chains of other chicken immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, goat, guinea pig, syrian hamster, horse, human, mouse, rabbit, rat and sheep serum proteins, but it may cross-react with immunoglobulins from other species.