Anti-IgG (human), mAb (rec.) Multiclonal (HRP)

Multiclonals are recombinant secondary antibodies that combine the best of polyclonal antisera and hybridoma monoclonal antibodies, while eliminating their disadvantages, plus they add the quality of recombinant reagents. Multiclonal antibodies consist of carefully adjusted mixtures recognizing different epitopes on all four different subclasses of human IgG. Their respective epitope binding sites do not compete with each other, therefore amplifying signal strengths. Multiclonals can contain up to 17 different individually tested monoclonal recombinant antibodies. This provides the typical advantage of polyepitope recognition which is key to the broad application profile of polyclonal antisera, but eliminates their disadvantages (limited batch sizes and batch-to-batch variations, no long-term reproducibility, undefined composition, unknown constituents). Multiclonals are completely sequence defined, implying their unlimited long-term availability and always identical test results. Their composition of individually characterised antibodies minimizes cross-reactivity with other targets, since they do not contain non-target directed IgG like all animal derived polyclonals do. This allows for a much lower unspecific binding reactivity in many assays compared to animal based products. This purified antibody panel is conjugated to horseradish peroxidase (HRP) and ideal for diagnostic and research applications. Protein function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins- secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). [The UniProt Consortium]