Recombinant Human CD16 protein (His tag)
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Recombinant Human CD16 protein (His tag) is a Human Fragment protein, in the 17 to 208 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE.
View Alternative Names
CD16a, CD16A, FCG3, FCGR3, IGFR3, FCGR3A, Low affinity immunoglobulin gamma Fc region receptor III-A, IgG Fc receptor III-A, CD16-II, CD16a antigen, Fc-gamma RIII-alpha, FcR-10, IgG Fc receptor III-2, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcgammaRIIIA
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human CD16 protein (His tag) (AB271508)
SDS-PAGE analysis of 3 μg ab271508.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This receptor plays a significant role in immune system regulation by contributing to the activation of immune effector cells. CD16 is not part of a larger complex but it operates in concert with CD3 proteins to trigger intracellular signaling pathways upon engagement with its ligand. Its function is important for the antibody-dependent clearance of infected or malignant cells from the body representing an essential linkage between innate and adaptive immunity.
Pathways
Signaling involving CD16 is integrated into the immune response mechanisms that include the Fc gamma receptor-mediated phagocytosis pathway. This pathway involves interactions with IgG antibodies and complements the activity of other Fc gamma receptors such as CD32 and CD64. Through these interactions CD16 enhances phagocytic activity and stimulates the secretion of cytokines and chemokines important for orchestrating an effective immune response.
Specifications
Form
Liquid
General info
Function
Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (PubMed : 11711607, PubMed : 21768335, PubMed : 22023369, PubMed : 24412922, PubMed : 25786175, PubMed : 25816339, PubMed : 28652325, PubMed : 8609432, PubMed : 9242542). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory-like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC (PubMed : 24412922, PubMed : 25786175). Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (PubMed : 29967280, PubMed : 9916693). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (PubMed : 1825220, PubMed : 23024279, PubMed : 2532305). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (PubMed : 10318937, PubMed : 23006327). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (PubMed : 27670158). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed : 34485821).. (Microbial infection) Involved in Dengue virus pathogenesis via antibody-dependent enhancement (ADE) mechanism. Secondary infection with Dengue virus triggers elevated levels of afucosylated non-neutralizing IgG1s with reactivity to viral envelope/E protein. Viral antigen-IgG1 complexes bind with high affinity to FCGR3A, facilitating virus entry in myeloid cells and subsequent viral replication.
Post-translational modifications
Glycosylated. Contains high mannose- and complex-type oligosaccharides. Glycosylation at Asn-180 is mandatory for high affinity binding to the Fc and for discrimination between fucosylated and afucosylated IgG glycoforms.. Undergoes rapid ectodomain shedding upon NK cell stimulation. The soluble form is produced by a proteolytic cleavage mediated by ADAM17. Repeated stimulation causes receptor shedding, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells while avoiding activation-induced NK cell apoptosis.. Phosphorylated at RSSTR motif by PKC. The relevant physiological PKCs might be PRKCI, PRKCG, PRKCE, PRKCH and PRKCQ.
Target data
Product promise
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