Secondary Antibodies

Anti-Rat IgG (H&L) generated in rabbit 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.

Anti-Rat IgG F(ab')2 Antibody generated in rabbit recognizes the dimeric Fab portion of the rat IgG molecule. Rat IgG F(ab')2 is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. F(ab')2 molecules lack the Fc portion of IgG and therefore receptors that bind rat IgG F(c) will not bind rat IgG F(ab')2 molecules. 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.

Anti-Rat IgM antibody generated in rabbit specifically detects rat IgM mu 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.

Anti-Sheep IgG (H&L) generated in rabbit detects sheep 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.

Anti-Sheep IgG F(ab')2 Antibody generated in rabbit recognizes the dimeric Fab portion of the sheep IgG molecule. Sheep IgG F(ab')2 is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. F(ab')2 molecules lack the Fc portion of IgG and therefore receptors that bind sheep IgG F(c) will not bind sheep IgG F(ab')2 molecules. 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.

Anti-Sheep IgM antibody generated in rabbit specifically detects Sheep IgM mu 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-Sheep IgM antibody is ideal for investigators in Immunology, Microbiology, and Cell Biology.

Anti-Sheep IgG (H&L) generated in donkey detects sheep 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.

Anti-Swine IgG (H&L) generated in rabbit detects swine 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.

Anti-Swine IgG F(ab')2 Antibody generated in rabbit recognizes the dimeric Fab portion of the Swine IgG molecule. Swine IgG F(ab')2 is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. F(ab')2 molecules lack the Fc portion of IgG and therefore receptors that bind Swine IgG F(c) will not bind Swine IgG F(ab')2 molecules. 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.