Anti ha antibody ha 11

Manufactured by Fortrea

The Anti-HA antibody (HA.11) is a laboratory reagent used for the detection and identification of proteins tagged with the HA (Hemagglutinin) epitope. This antibody specifically recognizes the HA tag, which is a commonly used epitope tag for recombinant protein expression and purification.

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Lab products found in correlation

Protein g sepharose 4b, by GE Healthcare (2 mentions) Protease inhibitor cocktail tablet, by Roche (1 mentions) Magnetic bead, by Merck Group (1 mentions) Pierce bca, by Thermo Fisher Scientific (1 mentions) Complete edta free tablet, by Roche (1 mentions) V5 antibody, by Merck Group (1 mentions) β actin, by Merck Group (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Phosstop, by Roche (1 mentions)

3 protocols using anti ha antibody ha 11

Immunoprecipitation of HCV Core Protein

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Each of the cell lines were seeded on six-well plates (one plate for each cell line) and were infected with lentiviruses expressing HCV core. After 48 h, the cells were collected, and the cell lysates were incubated with anti-HA antibody (HA.11, Covance, 1 μl per sample) at 4 °C for 90 min and then further incubated with Protein G Sepharose 4B (GE Healthcare) at 4 °C for 90 min. The beads were washed three times with lysis buffer, boiled at 95 °C for 5 min, and subjected to western blotting.

Aizawa S., Okamoto T., Sugiyama Y., Kouwaki T., Ito A., Suzuki T., Ono C., Fukuhara T., Yamamoto M., Okochi M., Hiraga N., Imamura M., Chayama K., Suzuki R., Shoji I., Moriishi K., Moriya K., Koike K, & Matsuura Y. (2016). TRC8-dependent degradation of hepatitis C virus immature core protein regulates viral propagation and pathogenesis. Nature Communications, 7, 11379.

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Ubiquitination of MCL1 Variants

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293T cells (2x10⁶) seeded on 10 cm dishes were transfected with 1.0 μg of either pCAGGS MCL1 or pCAGGS MCL1^K/R and 0.05 μg of HA-ubiquitin plasmid by using PEI after 12 h of incubation. After 2 days, cells were treated with proteasome inhibitor (20 μM, ALLN) for 6 h and lysed with buffer A (50 mM Tris-HCl [pH 7.4], 150 mM NaCl, 1 mM EDTA, 1% Triton X-100, 1% sodium deoxycholate, 1% SDS) supplemented with 1 mM sodium fluoride and protease inhibitor cocktail tablets (Roche) on ice for 30 min and sonicated. Cell lysates (200 μl) were diluted with buffer A lacking SDS, incubated with anti-HA antibody (HA.11, 2 μl per sample; Covance) at 4 °C for 90 min and then further incubated with Protein G Sepharose 4B (GE Healthcare) at 4 °C for 90 min. The beads were washed five times in buffer A lacking SDS and eluted in sample buffer after incubation at 95°C for 5 min. Denatured samples were resolved by SDS-PAGE and immunoblotting.

Suzuki T., Okamoto T., Katoh H., Sugiyama Y., Kusakabe S., Tokunaga M., Hirano J., Miyata Y., Fukuhara T., Ikawa M., Satoh T., Yoshio S., Suzuki R., Saijo M., Huang D.C., Kanto T., Akira S, & Matsuura Y. (2018). Infection with flaviviruses requires BCLXL for cell survival. PLoS Pathogens, 14(9), e1007299.

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Immunoprecipitation and Degradation Assay

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Cells were washed in PBS and lysed in NETN buffer, in the presence of phosphatase (PhosSTOP; Roche) and protease (Complete EDTA free tablets; Roche, Indianapolis, IN) inhibitors. The concentration of proteins were determined by PierceTM BCA (Thermo Scientific, Rockford, IL). Magnetic Beads (SIGMA-ALDRICH, St Louis, MO) were coated with anti-HA antibody (HA1.1, Covance) for 30min (RT). For immunoprecipitation, cell lysates were incubated with the beads coated with anti-HA for 1h at 4°C. Beads were washed 3 times with NETN buffer and proteins were eluted in Lamelli buffer and boil for 10min. Samples were subjected to SDS-PAGE on 4–12% acrylamide gel Criteron™ TGX gel (Bio-Rad, Hercules, CA) and transferred to PVDF membrane (EMD Millipore, Billerica, MA). For degradation assay, cells were lysed using SET buffer (1% SDS, 50mM tris-HCl, pH 7.4, 1mM EDTA) and boiled for 20min. Samples were resolves by SDS-PAGE as described above. V5 antibody (Sigma Aldrich), β-actin (Sigma Aldrich), rabbit polyclonal DCAF1 antibody was kindly provided by Dr. Ling-Jun Zhao (Saint Louis University).

DePaula-Silva A.B., Cassiday P.A., Chumley J., Bosque A., Monteiro-Filho C.M., Mahon C.S., Cone K.R., Krogan N., Elde N.C, & Planelles V. (2015). Determinants for degradation of SAMHD1, Mus81 and induction of G2 arrest in HIV-1 Vpr and SIVagm Vpr. Virology, 477, 10-17.

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