Cat#:PA-1853F;Product Name:Mouse Anti-Hamster IgG2 / IgG3 Antibody, HRP Conjugated;Synonym:Ig gamma-2 chain C region; immunoglobulin Gm2; immunoglobulin heavy constant gamma 2 (G2m marker); immunoglobulin heavy constant, gamma 2; FLJ39988; FLJ40587; FLJ40789; FLJ40834; HDC; MGC45809; DKFZp686H11213; FLJ40036; FLJ40253; Heavy chain disease protein; Ig gamma 3 chain C region; IGHG3; Immunoglobulin heavy constant gamma 3 (G3m marker); IgG2; Immunoglobulin G2; IgG2 γ2; Immunoglobulin G2 γ2; IgG2 heavy chain; Immunoglobulin G2 heavy chain; IgG2 γ2 heavy chain; Immunoglobulin G2 γ2 heavy chain; IgG3; Immunoglobulin G3; IgG3 γ3; Immunoglobulin G3 γ3; IgG3 heavy chain; Immunoglobulin G3 heavy chain; IgG3 γ3 heavy chain; Immunoglobulin G3 γ3 heavy chain; IgG2/IgG3; Immunoglobulin G2/ Immunoglobulin G3; Hamster IgG; Hamster IgG2/IgG3; Hamster Immunoglobulin G2/ Immunoglobulin G3;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-Hamster IgG2/IgG3 Monoclonal Antibody, HRP Conjugated;Host Species:Mouse;Species Reactivity:Hamster;Isotype:IgG2b;Application: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;
Ig gamma-2 chain C region; immunoglobulin Gm2; immunoglobulin heavy constant gamma 2 (G2m marker); immunoglobulin heavy constant, gamma 2; FLJ39988; FLJ40587; FLJ40789; FLJ40834; HDC; MGC45809; DKFZp686H11213; FLJ40036; FLJ40253; Heavy chain disease protein; Ig gamma 3 chain C region; IGHG3; Immunoglobulin heavy constant gamma 3 (G3m marker); IgG2; Immunoglobulin G2; IgG2 γ2; Immunoglobulin G2 γ2; IgG2 heavy chain; Immunoglobulin G2 heavy chain; IgG2 γ2 heavy chain; Immunoglobulin G2 γ2 heavy chain; IgG3; Immunoglobulin G3; IgG3 γ3; Immunoglobulin G3 γ3; IgG3 heavy chain; Immunoglobulin G3 heavy chain; IgG3 γ3 heavy chain; Immunoglobulin G3 γ3 heavy chain; IgG2/IgG3; Immunoglobulin G2/ Immunoglobulin G3; Hamster IgG; Hamster IgG2/IgG3; Hamster Immunoglobulin G2/ Immunoglobulin G3
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.