Product Name: CD16 Antibody [HO-80]
Species Reactivity: Human
Tested Applications: Flow, Func, IF
Applications: Functional Activity (Order SAF formulation)Flow Cytometry: 0.5-1 ug/million cells in 0.1mlImmunofluorescence: 0.5-1 ug/mlOptimal dilution of the CD16 antibody should be determined by the researcher.
User Note: Optimal dilutions for each application to be determined by the researcher
Predicted Molecular Weight:
Immunogen: PBL s from a NK-leukemia patient were used as the immunogen for the CD16 antibody.
Host Species: Mouse
Purification: Protein G affinity chromatography
Physical State: Liquid
CAS NO.: 1202055-32-0
Product: NMS-P715
Buffer: PBS with 0.1 mg/ml BSA and 0.05% sodium azide
Concentration: 0.2 mg/mL
Storage Conditions: Aliquot and Store at -20C. Avoid freez-thaw cycles.
Clonality: Monoclonal
Conjugate: Unconjugated
Alternate Names: Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, CD16A, FCG3, FCGR3, IGFR3
Accession NO.:
Protein Ino:
Official Symbol: FCGR3A
Geneid: 2214
Background: It recognizes CD16 (Fcgamma;RIII), the low-affinity receptor for IgG with an apparent molecular weight of 50-80kDa. Two similar genes represent CD16, CD16A (Fcgamma;RIIIA), which exists as a hetero-oligomeric polypeptide-anchored form in macrophages and NK cells and CD16B (Fcgamma;RIIIB), which exist as a monomeric GPI-anchored form in neutrophils. Furthermore, there are two known polymorphisms of CD16B, NA-1 and NA-2. Individuals homozygous for NA-2 show a lower phagocytic capacity compared with NA-1. CD16 binds IgG in the form of immune complexes and shows preferential binding of IgG1 and IgG3 isotypes and minimal binding of IgG2 and IgG4. Upon IgG binding, both CD16 isoforms initiate signal transduction cascades that lead to a variety of responses including antibody-dependent cell-mediated cytotoxicity (ADCC), phagocytosis, degranulation and proliferation.
PubMed ID:http://aac.asm.org/content/34/1/176.abstract
