Cat#:PA-1885F;Product Name:Mouse Anti-Rat Immunoglobulin G2a Antibody;Synonym:Immunoglobulin G2a; IgG2a; Immunoglobulin G2a; IgG2aγ2a; Immunoglobulin G2aγ2a; IgG2a heavy chain, Immunoglobulin G2a heavy chain; IgG2aγ2aheavy chain; Immunoglobulin G2aγ2aheavy chain;Background:Immunoglobulin G (IgG) are antibody molecules. Each IgG is composed of four peptide chains — two heavy chains γ and two light chains. Each IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. IgG molecules are synthesized and secreted by plasma B cells. IgG antibodies are large molecules of about 150 kDa composed of 4 peptide chains. It contains 2 identical heavy chains of about 50 kDa and 2 identical light chains of about 25 kDa, thus a tetrameric quaternary structure. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves, which together form the Y-like shape. Each end of the fork contains an identical antigen binding site. The Fc regions of IgGs bear a highly conserved N-glycosylation site. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6-linked sialic acid residues.;Description:Mouse Anti-Rat Immunoglobulin G2a Monoclonal Antibody;Host Species:Mouse;Species Reactivity:Rat;Isotype:IgG;Application:IFM, ELISA;Storage:Store antibody products at 2-8°C. For long term storage, aliquot and freeze at -20°C. Avoid repeated freeze/thaw cycles;Usage:For Lab Research Use Only;
Immunoglobulin G2a; IgG2a; Immunoglobulin G2a; IgG2aγ2a; Immunoglobulin G2aγ2a; IgG2a heavy chain, Immunoglobulin G2a heavy chain; IgG2aγ2aheavy chain; Immunoglobulin G2aγ2aheavy chain
Gene Introduction:
Immunoglobulin G (IgG) are antibody molecules. Each IgG is composed of four peptide chains — two heavy chains γ and two light chains. Each IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. IgG molecules are synthesized and secreted by plasma B cells. IgG antibodies are large molecules of about 150 kDa composed of 4 peptide chains. It contains 2 identical heavy chains of about 50 kDa and 2 identical light chains of about 25 kDa, thus a tetrameric quaternary structure. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves, which together form the Y-like shape. Each end of the fork contains an identical antigen binding site. The Fc regions of IgGs bear a highly conserved N-glycosylation site. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6-linked sialic acid residues.