Anti-Kappa light chain antibody [OX12] - BSA and Azide free,Abcam,AB244585
ab244585 is the carrier-free version of ab238470 . Want a custom formulation? This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact [email protected] Conjugation ready Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications. Use our conjugation kits for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold. Compatibility This product is compatible with the Maxpar ® Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar ® is a trademark of Fluidigm Canada Inc.
Host
Mouse
Reactivity
Rat
Application
Flow Cyt
Platform ID
BAB300188927
Abcam
Contact
Tel: +44 (0)1223 696000
Fax: +44 (0)1223 215 215
Email:
Specifications
Scientific Background
Target data V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed : 24600447). 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 : 20176268, PubMed : 22158414). 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). See full target information IGKV1D-16
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