4122 Results for: "Jackson Immunoresearch Lab"

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 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 human IgG. It also reacts with the light chains of other human 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, mouse, rabbit, rat and sheep 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 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 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

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 human IgG. It also reacts with the light chains of other human 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, 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 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 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 sheep IgG. It also reacts with the light chains of other sheep 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 rat IgM but not with rat IgG or the light chains of 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 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 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 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 human IgG. It also reacts with the light chains of other human immunoglobulins. No antibody was detected against the Fc portion of human 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 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 human IgG. It also reacts with the light chains of other human 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 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 the F(ab')2 /Fab portion of human IgG. It also reacts with the light chains of other human immunoglobulins. No antibody was detected against the Fc portion of human 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 bovine, horse and mouse 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 human IgG. It also reacts with the light chains of other human 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 and mouse 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 human IgG. It also reacts with the light chains of other human immunoglobulins. No antibody was detected against the Fc portion of human IgG or against non-immunoglobulin serum proteins. The antibody may cross-react with immunogloublins from other species.

Supplier: Jackson Immunoresearch Lab

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 antigen-binding assay and/or ELISA, the antibody reacts with the Fcµ portion of the human IgM heavy chain but not with human IgG, IgA, or the light chains of human immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with IgM 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 Fcµ portion of the human IgM heavy chain but not with human IgG, IgA, or the light chains of human 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 serum proteins, but it may cross-react with IgM 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 both human IgG and IgM. It also reacts with the light chains of other human 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 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 cat IgG. It also reacts with the light chains of other cat 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 whole molecule guinea pig IgG. It also reacts with the light chains of other guinea pig 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 cat IgG. It also reacts with the light chains of other cat 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 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 the Fc portion of cat IgG heavy chain but not with the Fab portion of cat 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.

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 guinea pig IgG. It also reacts with the light chains of other guinea pig immunoglobulins. No antibody was detected against the Fc portion of guinea pig IgG or against non-immunoglobulin serum proteins. The antibody may cross-react with immunogloublins 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 cat IgG. It also reacts with the light chains of other cat 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 F(ab')2 /Fab portion of cat IgG. It also reacts with the light chains of other cat immunoglobulins. No antibody was detected against the Fc portion of cat IgG or against non-immunoglobulin serum proteins. The antibody may cross-react with immunogloublins 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

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 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 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 sheep IgG heavy chain but not with the Fab portion of sheep 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 serum proteins, but it may cross-react with immunoglobulins from other species.