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Human fc blocker

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The Human Fc blocker is a laboratory reagent designed to block the Fc region of human immunoglobulin G (IgG) antibodies. It can be used to prevent non-specific binding of IgG to Fc receptors in various experimental settings.

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Lab products found in correlation

Anti human igg fc apc antibody, by BioLegend (2 mentions) Pe goat anti mouse igg antibody, by BioLegend (1 mentions) Human cd138 microbead, by Miltenyi Biotec (1 mentions) Foxp3 transcription factor intracellular staining kit, by Thermo Fisher Scientific (1 mentions) Lsrii flow cytometer, by BD (1 mentions) Human fc receptor binding inhibitor, by Thermo Fisher Scientific (1 mentions) Donkey anti mouse antibodies, by Jackson ImmunoResearch (1 mentions) Live dead fixable aqua, by Thermo Fisher Scientific (1 mentions) Lsrfortessa, by BD (1 mentions) Permeabilization solution, by BD (1 mentions) Cytoflex, by Beckman Coulter (1 mentions) Perm wash buffer, by BD (1 mentions) 7 aminoactinomycin d 7 aad, by BD (1 mentions)

6 protocols using human fc blocker

1

CAR T Cell Expression Analysis

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After 96 h of infection with CAR lentiviral, the T cells were analyzed for CAR expression using flow cytometry and immunofluorescence assay. The UCAR-T cells were blocked with human Fc blocker (cat# 564220, BD), followed by consecutive incubation with 5 µg/mL BCMA-mFc (CAR-hu388, CAR-h31 and CAR-h32) and CD47-hFc (CAR-hu404, CAR-h31 and CAR-h32) proteins, APC anti-human IgG Fc antibody (cat# 410711, Biolegend) and PE-goat anti-mouse IgG antibody (cat# 405307, Biolegend). PE-goat IgG isotype control antibody (cat# 403004, Biolegend) and APC Rat IgG2a, κ isotype control antibody (cat# 400511, Biolegend) was used as negative controls.
Lu Q., Li H., Wu Z., Zhu Z., Zhang Z., Yang D, & Tong A. (2024). BCMA/CD47-directed universal CAR-T cells exhibit excellent antitumor activity in multiple myeloma. Journal of Nanobiotechnology, 22, 279.
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2

Enrichment and Characterization of Primary Multiple Myeloma Cells

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Primary MM cells were obtained from newly diagnosed, relapsed, or post-treatment patients with multiple myeloma. Clinical samples were collected from the West China Hospital of Sichuan University following the hospital protocols. The primary MM cells were isolated and enriched by human CD138 Microbeads (cat# 130-051-301, Miltenyi Biotec) according to manufacture instructions. After blocking with human Fc blocker (cat# 564220, BD), hu388-hFc, hu404-hFc and h32-hFc fusions (50 nM) were incubated respectively with primary MM cells, and then stained with APC anti-human IgG Fc antibody (cat# 410711, Biolegend) and detected by flow cytometry.
Lu Q., Li H., Wu Z., Zhu Z., Zhang Z., Yang D, & Tong A. (2024). BCMA/CD47-directed universal CAR-T cells exhibit excellent antitumor activity in multiple myeloma. Journal of Nanobiotechnology, 22, 279.
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3

Immunophenotyping and Intracellular Cytokine Staining of PBMCs

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Initial immunophenotyping and intracellular cytokine staining of PBMCs collected at enrollment (uninfected baseline) were performed on a subset of 60 children (Immune = 18, Delayed Fever = 21, and Early Fever = 21) in two separate batches with a similar distribution of classes. PBMCs were thawed, washed in PBS with 4% fetal bovine serum (FACS buffer), blocked with human Fc Blocker (BD Biosciences) for 20 min, stained with a cell viability stain in PBS for 30 min followed by staining with B cell, T cell, and monocyte cell surface markers in FACS buffer for 30 min at 4°C (antibodies listed in Key Resources Table). Cells were fixed and permeabilized using the FoxP3/transcription factor intracellular staining kit (eBioscience) prior to staining with intracellular antibodies for 30 min (antibodies listed in Key Resources Table). A minimum of 100,000 gated cells were acquired on an LSR II flow cytometer (BD). Dead cells were excluded from the analysis. Flow cytometric analysis was done using FlowJo 10 software (TreeStar). p53 staining was also performed using the anti-p53 monoclonal antibody clone PAb240 on PBMCs of 9 additional children (Delayed Fever = 5, and Early Fever = 4).
Tran T.M., Guha R., Portugal S., Skinner J., Ongoiba A., Bhardwaj J., Jones M., Moebius J., Venepally P., Doumbo S., DeRiso E.A., Li S., Vijayan K., Anzick S.L., Hart G.T., O’Connell E.M., Doumbo O.K., Kaushansky A., Alter G., Felgner P.L., Lorenzi H., Kayentao K., Traore B., Kirkness E.F, & Crompton P.D. (2019). A molecular signature in blood reveals a role for p53 in regulating malaria-induced inflammation. Immunity, 51(4), 750-765.e10.
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4

Fc Receptor Expression Modulation

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Mouse monoclonal antibodies to CD16 (GRM1 and 3G8, mouse IgG1 BioLegend), CD32 (Fun2; AT10 mouse IgG1, BioRad; and 6C4, mouse IgG1, eBioscience, Rockford, IL), CD64 (clone 10.1), and CD89 (clone A59), mouse IgG1, IgG2a, and IgG2b (all from BioLegend), and human Fc blocker (BD Biosciences) or human Fc receptor binding inhibitor (eBioscience) diluted to a final concentration of 10 μg/ml were added to Mono Mac 6 cells in the presence or absence of CRP. At 48 h, the cells were resuspended and stained with 5 μg/ml propidium iodide and analyzed by flow cytometry. CRP and mouse monoclonal antibodies to CD32 (clone Fun2), CD64 (clone 10.1), or CD89 (clone A59) were also added to Mono Mac 6 cells in the presence or absence of 10 μg/ml donkey anti-mouse antibodies (Jackson ImmunoResearch) to cross-link the antibodies. At 48 h, the cells were resuspended and stained with 5 μg/ml propidium iodide and analyzed by flow cytometry.
Chen W., Pilling D, & Gomer R.H. (2017). C-reactive protein (CRP) but not the related pentraxins serum amyloid P and PTX3 inhibits the proliferation and induces apoptosis of the leukemia cell line Mono Mac 6. BMC Immunology, 18, 47.
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5

Phenotypic Analysis of CD4+ T cells

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CD4+ T cells after HSP or TCR culture were incubated with LIVE/DEAD® Fixable Aqua (ThermoFisher) and human Fc blocker (BD Bioscience). Then the cells were washed and stained with anti-CD4, CD8, CD27, and CD45RO- antibodies (Supplementary Data 8) on ice for 20 min. Transfected HEK 293T cells were suspended with PBS containing 1% FBS and 1 μg/mL 4’,6-diamidino-2-phenylindole (DAPI) before data acquisition. Fluorescence was measured on a BD LSRFortessa (Becton, Dickinson) and analyzed with FlowJo v10 (Becton, Dickinson).
Kobayashi-Ishihara M., Frazão Smutná K., Alonso F.E., Argilaguet J., Esteve-Codina A., Geiger K., Genescà M., Grau-Expósito J., Duran-Castells C., Rogenmoser S., Böttcher R., Jungfleisch J., Oliva B., Martinez J.P., Li M., David M., Yamagishi M., Ruiz-Riol M., Brander C., Tsunetsugu-Yokota Y., Buzon M.J., Díez J, & Meyerhans A. (2023). Schlafen 12 restricts HIV-1 latency reversal by a codon-usage dependent post-transcriptional block in CD4+ T cells. Communications Biology, 6, 487.
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6

Glioma Cell Surface Phenotyping by Flow Cytometry

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Glioma cells were analyzed by flow cytometry to identify Tim-3, Gal-9, and NLRC4 inflammasome-related molecules on their surfaces. The Fc receptor was blocked with human Fc blocker (BD Biosciences, San Jose, CA, USA). The glioma cell lines were then stained with the antibodies listed in Table S3.
The expression levels of intracellular molecules including Iba1, GFAP, and caspase-1 were determined by intracellular staining. Si-Tim-3 or si-Gal-9 was prepared and the cells were collected on day 3 and treated with permeabilization solution (BD Biosciences) at room temperature for 20 min. The cells were then washed with Perm/Wash Buffer (BD Biosciences) and stained at 4 °C for 30 min with the antibodies listed in Table S3. To exclude dead cells from the flow cytometry data, the cells were stained with 7-amino-actinomycin D (7-AAD; BD Pharmingen, San Diego, CA, USA) at a concentration of 5 μL/106 cells). The 7-AAD-negative glioma cell populations were analyzed. CytoFLEX (Beckman Coulter Inc., Brea, CA, USA) was used for all flow cytometry assays. All data were analyzed with FlowJo v. 10 (FlowJo LLC, Ashland, OR, USA).
Sim J., Park J., Kim S., Hwang S., Sung K., Lee J.E., Yang S., Cho K., Lee S., Moon J.S., Ahn J, & Lim J. (2022). Association of Tim-3/Gal-9 Axis with NLRC4 Inflammasome in Glioma Malignancy: Tim-3/Gal-9 Induce the NLRC4 Inflammasome. International Journal of Molecular Sciences, 23(4), 2028.
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