CD64 (FcγRI), one of the Fc receptors for IgG, is a membrane glycoprotein that mediates endocytosis, phagocytosis, antibody-dependent cellular cytotoxicity, cytokine release, and superoxide production. CD64 is also structurally distinct, containing an extracellular Ig-interactive region of three Ig-like domains in contrast to the two domains of the low affinity receptors FcγRII and FcγRIII. It is normally expressed on the surfaces of monocytes and macrophages.
β-2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules, involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases, various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.
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. 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. Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells.
Lascia la tua email e seleziona le aree che vuoi seguire per ricevere novita di prodotto, approfondimenti tecnici e promozioni piu pertinenti.
Puoi scegliere le macro-aree Life Science e Diagnostica oppure le singole specializzazioni.
Seleziona uno o piu ambiti di interesse per ricevere comunicazioni piu utili e mirate.
Aggiornamenti su ricerca, strumentazione e applicazioni per il mondo Life Science.
Novita, approfondimenti e promozioni per laboratori diagnostici e flussi operativi.
2025 TEMA Ricerca - All Rights Reserved.
