The recombinant protein L produced by aladdin is expressed in a prokaryotic system, purified, sterilized, and filtered. It can bind to various immunoglobulins through kappa chains, with a molecular weight of 35.4 kDa. Compared with protein A and protein G, protein L can bind to antibodies from various sources and subtypes more widely, including humans, mice, rats, rabbits, and chickens, but does not bind to immunoglobulin from cattle, dogs, goats, or sheep sources. Recombinant protein L can be widely used in the preparation of antibody affinity chromatography columns, affinity magnetic beads, ELISA assays, etc. It is commonly used for purification of antibodies or antibody fragments, labeling of indicators (such as fluorescence, enzymes, colloidal gold, biotin), etc.
规格
产品名称
Recombinant Protein L
别名
重组蛋白L | 重组大消化链球菌蛋白L | 重组蛋白L
英文别名
ProteinL | RPL | Recombinant Peptostreptococcus magnus Protein L | Peptostreptococcus magnus Protein L | Protein L
规格或纯度
无动物源,无载体,His标签,≥90%(SDS-PAGE),见COA
生化机理
Protein L is a 36,000 dalton immunoglobulin-binding protein isolated from the bacteria Peptostreptococcus magnus. Unlike Protein A and Protein G, which bind to the Fc region of immunoglobulins (antibodies), Protein L binds antibodies through light chain interactions. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (ScFv) and Fab fragments also bind to Protein L. Despite this wide binding range, Protein L is not a universal antibody-binding protein. Protein L binding is restricted to those antibodies that contain kappa light chains and it is only effective in binding certain subtypes of kappa light chains - about 65% of human immunoglobulins carry kappa light chains. Given these specific requirements for effective binding, the main application for immobilized Protein L is purification of monoclonal antibodies from ascites or cell culture supernatant that are known to have the kappa light chain. Protein L is extremely useful for purification of VLkappa-containing monoclonal antibodies from culture supernatant because it does not bind bovine immunoglobulins, which are often present in the media as a serum supplement. Also, Protein L does not interfere with the antigen-binding site of the antibody, making it useful for immunoprecipitation assays, even using IgM.