ADCP Bioassay Effector Cell FcγRIIa (R variant) -NFAT/Jurkat

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RQP74004
I. Background

Antibody-dependent cell-mediated phagocytosis (ADCP) is one of the important mechanisms of action for antibody drug development. FcγRIIa is the predominant Fcγ receptor involved in the ADCP process. FcγRIIa is expressed in myeloid effector cells, including macrophages and neutrophils, where it plays a role in the activation of these effector cells. Several clinical studies have studied the correlation of a FcγRIIa polymorphism (R131H) and the response to IgG1 subclass monoclonal antibodies (mAbs) such as rituximab. Engineered amino-acid substitutions in Fc-mAbs have been developed to enhance the mAb-mediated phagocytosis of tumor cells by macrophages.

 
II. Description

Recombinant Jurkat T cell expressing a firefly luciferase gene under the control of NFAT response elements with constitutive expression of human FcγRIIa, Histidine variant.

 
III. Introduction
Host Cell: Jurkat
Expressed gene: NFAT-Luc-FcγRIIa
Stability: 32 passages
Synonym(s): N/A
Freeze Medium: 90% FBS+10% DMSO
Culture Medium: 1640+10%FBS+800ug/ml hygromycin+1ug/ml puromycin
Mycoplasma Testing: The cell line has been screened using the PCR-based VenorGeM Mycoplasma Detection kit (Sigma-Aldrich, cat. #MP0025) to confirm the absence of Mycoplasma species.
Storage: Immediately upon receipt, store in liquid nitrogen.
Application(s): Characterize the Fc effector function of antibodies.
 
IV. Description of Host Cell Line
Organism: Human
Tissue: Peripheral blood
Disease: Childhood T acute lymphoblastic leukemia
Morphology: Lymphoblast
Growth Properties: Suspension
 
Ⅴ. Representative Data

Figure1.Recombinant Jurkat T cell expressing firefly luciferase gene under the control of NFAT response elements with constitutive expression of  human FcγRIIa, Histidine variant.

       

 Figure 2:Detect Luciferase assay by Promega Bright-Glo Luciferase Assay System. ADCP Bioassay Effector Cell FcγRIIa(R variant) -NFAT/Jurkat cells were stimulated by FcγRIIa (R variant), the S/B was 29.3-fold.