| Description | Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.Product Citations:Franco, Andrea, et al. "Human Fc Receptor–Like 5 Binds Intact IgG via Mechanisms Distinct from Those of Fc Receptors."The Journal of Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.Product Citations:Franco, Andrea, et al. "Human Fc Receptor–Like 5 Binds Intact IgG via Mechanisms Distinct from Those of Fc Receptors."The Journal of Immunology 190, no. 11 (2013): 5739-5746.Baković, Maja Pučić, et al. "High-Throughput IgG Fc N-Glycosylation Profiling by Mass Spectrometry of Glycopeptides." Journal of proteome research 12, no. 2 (2013): 821-831Barb, Adam W., et al. "NMR Characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation." Biochemistry 51, no. 22 (2012): 4618-4626.Padmanabhan A, et al. Intravenous immunoglobulin for the treatment of severe refractory heparin induced thrombocytopenia. Chest, Available online 17 April 2017 in press, corrected proof.Anquetil F, et al. IgM and IgA Rheumatoid Factors Purified from Rheumatoid Arthritis Sera Boost the Fc Receptor– and Complement-Dependent Effector Functions of the Disease-Specific Anti–Citrullinated Protein Autoantibodies. J Immunol. 2015 Apr 15;194(8):3664-74. doi: 10.4049/jimmunol.1402334. Epub 2015 Mar 13.Frank M, et al. Immunoglobulin G1 Fc domain motions: implications for Fc engineering. J Mol Biol. 2014 Apr 17;426(8):1799-811. doi: 10.1016/j.jmb.2014.01.011. Epub 2014 Feb 9.Ref: Ricardo, M.J. et al. 1984. Clinical Diagnosis and Management by Laboratory Methods (J.B. Henry, ed.), 860; Poljak, R. J. 1985. Methods Enzymol. 116, 190... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (By similarity).Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (By similarity).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. 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 (By similarity).Fc-binding subunit that associates with 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 (By similarity).Mediates enhanced ADCC in response to afucosylated IgGs... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptors that recognize the Fc portion of IgG are divided into three groups designated Fc gamma RI, RII, and RIII, also known respectively as CD64, CD32, and CD16. Fc gamma RI binds IgG with high affinity Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptors that recognize the Fc portion of IgG are divided into three groups designated Fc gamma RI, RII, and RIII, also known respectively as CD64, CD32, and CD16. Fc gamma RI binds IgG with high affinity and functions during early immune responses. Fc gamma RII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses.High affinity immunoglobulin gamma Fc receptor I is also known as FCGR1A, FCG1, FCGR1, CD64 and IGFR1, is a type of integral membrane glycoprotein that binds monomeric IgG-type antibodies with high affinity, which belongs to the immunoglobulin superfamily or FCGR1 family. FCGR1A / CD64 contains 3 Ig-like C2-type (immunoglobulin-like) domains. CD64 is constitutively found on only macrophages and monocytes, but treatment of polymorphonuclear leukocytes with cytokines like IFNγ and G-CSF can induce CD64 expression on these cells... Read More | Purity≥ 98% SDS-PAGE.FunctionInvolved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. Stimulates glucose uptake in adipocytes. Activity requires the presence of KLB | Purity> 97 % by SDS-PAGE and HPLC analyses.FunctionReceptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation whichPurity> 97 % by SDS-PAGE and HPLC analyses.FunctionReceptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase... Read More |