![]() So, they can provide excellent sensitivity combined with superior specificity and reproducibility, only available from a recombinant antibody. Recombinant multiclonal antibodies are a defined mixture of carefully selected individual recombinant monoclonal antibodies designed to recognize different epitopes on the same antigen. For applications where a polyclonal antibody would traditionally be used (eg, when analyzing low-abundance targets or detecting multiple post-translational modifications at once), recombinant multiclonal antibodies can offer an ideal solution. We recommend using recombinant monoclonal antibodies when a suitable clone exists for your particular target and application to ensure experimental reproducibility and long-term antibody supply. Since the antibody-encoding sequence is known and defined, it can be further engineered and manipulated for its intended use. Compared to traditional monoclonal and polyclonal antibodies, recombinant antibodies offer long-term, secured supply with a minimal batch-to-batch variation. The term 'recombinant' refers to antibodies produced in vitro using synthetic genes. Monoclonal antibodies have high specificity for their target, low non-specific cross-reactivity, and minimal batch-to-batch variations. In contrast to polyclonal antibodies, monoclonal antibodies only recognize a single epitope per antigen. However, they are limited in supply, subject to high batch-to-batch variability, and exhibit cross-reactivity and lack of specificity. ![]() By binding to several different epitopes, polyclonal antibodies can produce a strong signal against the target antigen in their relevant application and are not biased against a single epitope. To recap, polyclonal antibodies consist of a heterogeneous mixture of antibodies, with each antibody recognizing different epitopes of a particular antigen. These antibodies have distinct advantages and limitations covered here. When choosing a primary antibody, consider the following: Antibody clonality and manufacture methodĬlonality is determined by whether the antibodies come from different B-cells (polyclonal antibodies) or identical B-cells derived from a parent clone (monoclonal antibodies). So overall, in general terms, antibody specificity helps us discuss if the antibody that we are using in our research (whether it’s a single antibody from a B cell or a pool of antibodies from serum) is able to detect our target protein specifically without cross-reacting with non-specific proteins.A primary antibody is an antibody that binds directly to a target protein, with a variable antibody region recognizing a protein's epitope. ![]() Techniques for increasing specificity will be discussed on the Monoclonal Antibody Alternative page. These two antibody production techniques will be discussed on the Polyclonal vs Monoclonal Antibodies page.Īlso, because serum contains antibodies against so many antigens (not just the protein that may have been used for immunizations), specificity is typically very low with raw serum. This brings up the issue of how antibodies are typically used, since they can be collected directly from the serum or by isolating the B cell(s) that is producing the antibody of interest. So, one antibody could potentially recognize two or more proteins if these proteins are highly homologous and contain the same epitope.Īlso, it is important to recognize that multiple antibodies will be generated against a typical protein antigen and so any one of these antibodies could potentially cross-react with another protein that contains the same epitope(s). ![]() However, it is important to recognize that a particular epitope could potentially appear on more than one protein antigen. This specificity allows precise detection of a target antigen such as a protein while avoiding detection of unrelated proteins that are not of interest. Each individual antibody protein is capable of binding specifically with one unique epitope thanks to the unique Antigen Binding Site located at the tip of the variable region on the antibody.
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