Mouse anti ha agarose beads

Manufactured by Merck Group

Mouse anti-HA agarose beads are a laboratory product used for the purification and detection of proteins tagged with the hemagglutinin (HA) epitope. They consist of agarose beads coated with monoclonal antibodies specific to the HA tag. These beads can be used to capture and isolate HA-tagged proteins from cell lysates or other samples.

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Lab products found in correlation

Ha peptide, by Merck Group (1 mentions) Mouse igg beads, by Merck Group (1 mentions) Mouse anti flag m2 agarose beads, by Merck Group (1 mentions)

Close spelling variants of this product

Agarose (759 citations) Anti-HA (475 citations) Mouse anti-HA (118 citations) Anti-HA agarose (100 citations) Agarose beads (61 citations) Anti-HA beads (54 citations) HA-agarose beads (26 citations) HA beads (22 citations) Mouse anti-HA agarose (3 citations)

3 protocols using mouse anti ha agarose beads

Immunoprecipitation of NPM1-HA and C11orf98-FLAG

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HEK293T cells were cotransfected
with C11orf98-FLAG and NPM1-HA (empty vector as a control). Lysates
from both samples were incubated with mouse anti-HA agarose beads
(Sigma, catalog no. A2095) to immunoprecipitate HA-tagged NPM1. Alternatively,
lysates from HEK293T cells co-expressing C11orf98-FLAG and NPM1-HA
were incubated with either mouse IgG beads (Sigma, catalog no. A0919)
or mouse anti-HA agarose beads. After being washed three times with
TBST, bound proteins were eluted with HA peptide (Sigma, catalog no.
I2149) at 4 °C for 1 h. The eluents were then separated by SDS–PAGE
and analyzed by Western blotting using the indicated antibodies.

Chu Q., Rathore A., Diedrich J.K., Donaldson C.J., Yates JR I.I.I, & Saghatelian A. (2017). Identification of Microprotein–Protein Interactions via APEX Tagging. Biochemistry, 56(26), 3299-3306.

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HA-tagged RhoB Interactome Profiling

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For HA-tag immunoprecipitation, pmCherryC1-RhoB, pmCherryC1-RhoB-T19N, or pmCherryC1-RhoB-G14V (gift of N. Reinhard, Swammerdam Institute for Life Sciences, Amsterdam, Netherlands) was cotransfected with NTAP-HA-CUL3 (gift of H. Genau, Goethe University Medical School, Frankfurt am Main, Germany). For native coimmunoprecipitation, transfected cells were lysed in lysis buffer (150 mM NaCl, 50 mM Tris, pH 7.4, 1 mM EDTA, 5% glycerol, and 1% IGEPAL) supplemented with protease inhibitor complex (Roche). Lysates were cleared by centrifugation and incubated with mouse anti-HA agarose beads (Sigma) for 3 h at 4°C. Upon incubation, beads were washed four times with the lysis buffer and boiled in 50 μl sample buffer, and samples were analyzed by immunoblotting.

Kovačević I., Sakaue T., Majoleé J., Pronk M.C., Maekawa M., Geerts D., Fernandez-Borja M., Higashiyama S, & Hordijk P.L. (2018). The Cullin-3–Rbx1–KCTD10 complex controls endothelial barrier function via K63 ubiquitination of RhoB. The Journal of Cell Biology, 217(3), 1015-1032.

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Immunoprecipitation of Tagged Proteins

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HEK293T lysates were prepared by sonication in phosphate-buffered saline (PBS) containing 0.1% Triton X-100 and 0.5% protease inhibitor cocktail (Calbiochem) according to a method described elsewhere [38] (link). Proteins in the lysate were immunoprecipitated (IP) with mouse anti-HA agarose beads (Sigma, A2095) or mouse anti-Flag M2 agarose beads (Sigma, A2220) for 2 h at 4˚C. After immunoprecipitation, proteins bound to the beads were washed three times with PBS containing 0.1% Triton X-100, eluted with 30 μl 2× electrophoresis sample buffer, and detected by immunoblotting (IB) according to a method described elsewhere [38] (link).

Li Y.J., Chen C.Y., Kuo Y.S., Huang Y.W., Kuo R.L., Chang L.K., Yang J.H., Lai C.H., Shih S.R, & Chiu Y.F. (2024). OTUB1 contributes to the stability and function of Influenza A virus NS2. PLoS pathogens, 20(5).

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