Anti ha antibody

Manufactured by R&D Systems

The Anti-HA antibody is a research tool used to detect the presence of the hemagglutinin (HA) tag in recombinant proteins. It is a highly specific antibody that binds to the HA epitope, allowing researchers to identify and track HA-tagged proteins in various experimental procedures.

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5 protocols using anti ha antibody

B Cell Cytokine Stimulation Protocol

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All cells were maintained in RPMI‐1640 medium (Sigma–Aldrich, Buchs, Switzerland) supplemented with 10% heat‐inactivated (hi) fetal bovine serum (FBS; Life Technologies‐Thermo Fisher Scientific, Reinach, Switzerland), 2 mM l‐glutamine, and 100 U/mL penicillin, and 100 μg/mL streptomycin, referred to hereafter as cRPMI. All cells were cultured at 37°C in 5% CO₂ air with a relative humidity >95%. B cells were stimulated with recombinant human IL‐4 (100 ng/mL), IL‐10 (100 ng/mL), IL‐13 (100 ng/mL), IL‐17A (100 ng/mL), IL‐22 (100 ng/mL), TGF‐β1 (10 ng/mL), and IFN‐γ (50 ng/mL, all Peprotech). Stimulation with HA‐tagged recombinant human CD40 Ligand (CD40L; 500 ng/mL) was complemented with anti‐HA antibody (200 ng/mL, both R&D Systems) enabling multimer formation. Hemozoin (LabForce AG) was used at 200 μg/mL.

Summerauer A.M., Jäggi V., Ogwang R., Traxel S., Colombo L., Amundsen E., Eyer T., Subramanian B., Fehr J., Mantel P., Idro R, & Bürgler S. (2022). Epstein–Barr virus and malaria upregulate AID and APOBEC3 enzymes, but only AID seems to play a major mutagenic role in Burkitt lymphoma. European Journal of Immunology, 52(8), 1273-1284.

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Stimulation of BCP-ALL Cells

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BCP-ALL-cells were stimulated with recombinant human IL-13 (100 ng/ml), recombinant human TGF-β1 (10 ng/ml), and recombinant IFN-γ (50 ng/ml, all Peprotech). Stimulation with HA-tagged recombinant human CD40 Ligand (CD40L) (500 ng/ml) was complemented with anti-HA antibody (200 ng/ml, both R&D Systems) enabling multimer formation.

Traxel S., Lehmann J., Richard S., Sidorov S., Niggli F., Berger C., Nadal D, & Bürgler S. (2021). Support of BCP-ALL-cells by autologous bone marrow Th-cells involves induction of AID expression but not widespread AID off-target mutagenesis. Cancer Immunology, Immunotherapy, 70(8), 2275-2289.

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Dendritic Cell Activation and Tumor Cell Assay

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Monocytes isolated from PBMCs using human CD14 positive selection kit (Stemcell) were cultured in X-Vivo-15 media (Lonza) with 2% human AB serum (Invitrogen), 1000 IU/mL human GM-CSF and 500 IU/mL human IL-4 (Peprotech) for 6 days. Fresh culture media containing GM-CSF and IL-4 were added on day 3. The resulting monocyte-derived dendritic cells (mDCs) were collected and seeded at 1 × 10⁶ cells/well in 12-well plates. Cells were activated with 0.5 μg/mL of HA-tagged CD40L (R&D systems) and 2 μg/ml of anti-HA antibody (R&D systems); and treated with selumetinib or DMSO control for a further 2 days.
2 × 10⁵ CT26 cells were cultured overnight prior to treatment with selumetinib or DMSO control for 2 days.
For flow cytometry analysis, mDCs were stained with fixable LIVE/DEAD violet (Life Technologies) and incubated with human TruStain FcX (Biolegend) before addition of: CD80-FITC (clone L307.4); CD83-PE (clone HB15e); CD86-APC (clone FUN-1) (BD Biosciences); HLA-DR-PE (clone L243, eBioscience). CT26 cells were stained with a viability stain, H2-Kd-PE (clone SF1–1.1) and PD-L1-APC (clone 10F.9G2, Biolegend). Stained cells were analyzed using a FACScantoII (BD Biosciences).

Poon E., Mullins S., Watkins A., Williams G.S., Koopmann J.O., Di Genova G., Cumberbatch M., Veldman-Jones M., Grosskurth S.E., Sah V., Schuller A., Reimer C., Dovedi S.J., Smith P.D., Stewart R, & Wilkinson R.W. (2017). The MEK inhibitor selumetinib complements CTLA-4 blockade by reprogramming the tumor immune microenvironment. Journal for Immunotherapy of Cancer, 5, 63.

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Quantitative Protein Analysis via SDS-PAGE

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To quantify the total amount of a protein, cells were grown to mid-log phase and lysed by FastPrep-24 5G device. For quantification equal amounts of total protein were separated by SDS-PAGE, and proteins were detected with the corresponding primary antibody, a horse radish peroxidase-coupled secondary antibody and CheLuminate-HRP ECL solution (Applichem). Chemiluminescence signals were imaged using a ChemoCam Imager (Intas) and quantified using FIJI. Mex67 and Hpr1 were HA-tagged and detected with an anti-HA antibody fused with HRP (R&D Systems). The antibody directed against Sto1/Cbp80 is a kind gift of D. Görlich (36 (link)).

Keil P., Wulf A., Kachariya N., Reuscher S., Hühn K., Silbern I., Altmüller J., Keller M., Stehle R., Zarnack K., Sattler M., Urlaub H, & Sträßer K. (2022). Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA. Nucleic Acids Research, 51(2), 831-851.

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Multifactorial B Cell Stimulation

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All cells were maintained in RPMI-1640 medium (Sigma-Aldrich, Buchs, Switzerland) supplemented with 10% heat-inactivated (hi) fetal bovine serum (FBS; Life Technologies-Thermo Fisher Scientific, Reinach, Switzerland), 2 mM L-glutamine, and 100 U/mL penicillin, and 100 μg/mL streptomycin, referred to hereafter as cRPMI. All cells were cultured at 37°C in 5% CO₂ air with a relative humidity >95%. B cells were stimulated with recombinant human IL-4 (100 ng/mL), IL-10 (100 ng/mL), IL-13 (100 ng/mL), IL-17A(100 ng/mL), IL-22 (100 ng/mL), TGF-β1 (10 ng/mL), and IFN-γ (50 ng/mL, all Peprotech). Stimulation with HA-tagged recombinant human CD40 Ligand (CD40L; 500 ng/mL) was complemented with anti-HA antibody (200 ng/mL, both R&D Systems) enabling multimer formation. Hemozoin (LabForce AG) was used at 200 μg/mL.

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