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Anti ha

Manufactured by Applied Biological Materials
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The Anti-HA is a laboratory reagent used to detect and purify proteins that are tagged with the Hemagglutinin (HA) epitope. It is a monoclonal antibody that specifically binds to the HA tag, enabling the identification and isolation of HA-tagged proteins from complex samples.

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Lab products found in correlation

Anti flag hrp, by Merck Group (4 mentions) Anti flag, by Merck Group (4 mentions) Anti rac1, by Merck Group (3 mentions) Anti rhogdi1, by Santa Cruz Biotechnology (3 mentions) Anti ha hrp, by Roche (3 mentions) Anti cdc42, by BD (3 mentions) Anti flag, by Applied Biological Materials (2 mentions) Ha peptide, by Merck Group (2 mentions) Anti v5, by Thermo Fisher Scientific (2 mentions) Anti ephrinb, by Santa Cruz Biotechnology (2 mentions) α tubulin, by Merck Group (2 mentions) Anti ephrinb1, by R&D Systems (2 mentions) Protein a g agarose bead, by Santa Cruz Biotechnology (2 mentions) Anti gst, by Santa Cruz Biotechnology (2 mentions) Anti rhoa, by Santa Cruz Biotechnology (2 mentions) Anti acetylated lysine, by Cell Signaling Technology (1 mentions) Anti ubiquitin, by Merck Group (1 mentions) Anti p300, by BD (1 mentions) Anti myc, by Applied Biological Materials (1 mentions) Anti α tubulin, by Merck Group (1 mentions)

Spelling variants of this product

Anti-mouse HA tag monoclonal antibody (2 citations) Anti-HA epitope (2 citations) Rabbit anti-HA (2 citations) Mouse anti-HA (2 citations)

7 protocols using anti ha

1

Immunoblot and Immunostaining Antibodies

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Antibodies used for the immunoblot and immunostaining were anti-p300 (BD Biosciences, San Jose, CA, USA), anti-α-tubulin (Sigma), anti-myc, anti-Flag, anti-GFP, anti-HA (abm, Richmond, Canada), anti-ubiquitin (Millipore, Billerica, MA, USA), anti-acetylated lysine (Cell signaling, Danvers, MA, USA). Anti-HIPK2 antibody was a kind gift of Dr. K. Isono (RIKEN, Japan) and described previously27 (link).
Choi J.R., Lee S.Y., Shin K.S., Choi C.Y, & Kang S.J. (2017). p300-mediated acetylation increased the protein stability of HIPK2 and enhanced its tumor suppressor function. Scientific Reports, 7, 16136.
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2

Co-Immunoprecipitation of HA-tagged Rrp6p

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Samples were grown and harvested as previously stated. Cell lysates were prepared as indicated above, but with the Co-IP lysis buffer (50mM Tris-HCl pH 7.4, 50mM NaCl and 1% NP-40) supplemented with protease and phosphatase inhibitors (Roche). Approximately 1.5mg of protein lysates were incubated with 25uL of magnetic anti-HA beads (Pierce) for 1 h at 4°C. Samples were washed 6 times with lysis buffer and eluted in 40uL of 1 mg/mL HA Peptide (Sigma-Aldrich). 10uL of eluate and 5ug of total lysates were loaded onto each lane of a Nu-Page gel. Rrp6p was detected with anti-Rrp6 (1:5000, (Schuch et al., 2014 )) and HA tagged proteins were detected with anti-HA (1:5000, ABM). Secondary antibodies used were obtained from LI-COR (1:10000).
Wang C., Liu Y., DeMario S.M., Mandric I., Gonzalez-Figueroa C, & Chanfreau G.F. (2020). Rrp6 Moonlights in an RNA Exosome-Independent Manner to Promote Cell Survival and Gene Expression during Stress. Cell reports, 31(10), 107754.
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3

Immunoprecipitation and Immunoblotting Assay

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Cells were harvested in lysis buffer (20 Mm Tris-HCl pH 8, 137 mM NaCl, 2 mM EDTA and 1% NP-40) with protease inhibitor cocktail at 4°C. Equal amounts of protein lysates were incubated with control IgG, anti-HA (ABM, G036), anti-Flag (Sigma, F1804), or anti-ephrinB1 (R&D systems, AF473) at 4°C overnight under mild agitation. Protein A/G-agarose beads (Santa Cruz Biotechnology) were then incubated for 1hr, followed by washing three times with lysis buffer. Immunoprecipitates and total protein lysates were separated by SDS-PAGE and immunoblotted with anti-HA-HRP (Roche, 12013819001), anti-Flag-HRP (Sigma, A8592), anti-V5 (Invitrogen, R961-25), anti-ephrinB1 (R&D Systems, af473) or anti-ephrinB (Santa Cruz Biotechnology C18, SC-910), anti-EphB2 (R&D Systems, AF467), anti-RhoGDI1 (Santa Cruz Biotechnology, SC-360) and anti-RhoA (Santa Cruz Biotechnology, SC-418), anti-Rac1 (Millipore, 05-389), anti-Cdc42 (BD Bioscience, 610929) and α-tubulin (Sigma, T6199).
Cho H.J., Hwang Y.S., Yoon J., Lee M., Lee H.G, & Daar I.O. (2017). EphrinB1 promotes cancer cell migration and invasion through the interaction with RhoGDI1. Oncogene, 37(7), 861-872.
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4

Antibody Selection for Protein Detection

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The following antibodies were used: anti-FLAG, anti-FLAG-HRP, anti-HA, anti-HA-HRP (Sigma Aldrich), anti-FLAG, anti-HA, anti-GST (abm), anti-GST, anti-His (Santa cruz biotechnology), anti-H1, H2A, H2B (Abcam) and anti-H3, H4, H3K9Ac, H3K27Ac, H3K4me3, H3K9me2, H3K27me2 (Upstate).
Lee W.K, & Cho M.H. (2016). Telomere-binding protein regulates the chromosome ends through the interaction with histone deacetylases in Arabidopsis thaliana. Nucleic Acids Research, 44(10), 4610-4624.
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5

Protein Immunoprecipitation and Immunoblotting

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Cells were harvested in ice-cold RIPA buffer (100 mM Tris–HCl pH 7.6, 50 mM NaCl, 50 mM β-glycerophosphate, 50 mM NaF, 0.1 mM Na3VO4, 0.5% NP-40, 0.5% sodium deoxycholate and 5 mM EDTA) with protease inhibitor cocktail. Quantified protein lysates were incubated with anti-Flag (Sigma, F1804) and anti-HA (ABM, G036) at 4 °C overnight, followed by agarose beads were incubated for 2 h. Total protein lysates and immunoprecipitates were subjected to immunoblotting with anti-Flag-HRP (Sigma, A8592), anti-HA-HRP (Roche, 12013819001), anti-PLK1 (Cell Signaling Technology, 4513), anti-PLK1 (Santa Cruz Biotechnology, sc-17783), anti-RhoGDI1 (Santa Cruz Biotechnology, sc-373724), anti-RhoGDI1 (invitrogen, 51-1000Z), anti-GST (Santa Cruz Biotechnology, sc-138), anti-His (Santa Cruz Biotechnology, sc-8036), anti-Phospho-(Ser/Thr) (Cell Signaling Technology, 9631), anti-RhoA (Santa Cruz Biotechnology, sc-418), anti-Rac1 (Millipore, 05-389), anti-Cdc42 (BD Bioscience, 610929) and β-Actin (Santa Cruz Biotechnology, sc-47778).
Lim J., Hwang Y.S., Yoon H.R., Yoo J., Yoon S.R., Jung H., Cho H.J, & Lee H.G. (2024). PLK1 phosphorylates RhoGDI1 and promotes cancer cell migration and invasion. Cancer Cell International, 24, 73.
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6

Co-Immunoprecipitation of HA-tagged Rrp6p

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Samples were grown and harvested as previously stated. Cell lysates were prepared as indicated above, but with the Co-IP lysis buffer (50mM Tris-HCl pH 7.4, 50mM NaCl and 1% NP-40) supplemented with protease and phosphatase inhibitors (Roche). Approximately 1.5mg of protein lysates were incubated with 25uL of magnetic anti-HA beads (Pierce) for 1 h at 4°C. Samples were washed 6 times with lysis buffer and eluted in 40uL of 1 mg/mL HA Peptide (Sigma-Aldrich). 10uL of eluate and 5ug of total lysates were loaded onto each lane of a Nu-Page gel. Rrp6p was detected with anti-Rrp6 (1:5000, (Schuch et al., 2014 )) and HA tagged proteins were detected with anti-HA (1:5000, ABM). Secondary antibodies used were obtained from LI-COR (1:10000).
Wang C., Liu Y., DeMario S.M., Mandric I., Gonzalez-Figueroa C, & Chanfreau G.F. (2020). Rrp6 Moonlights in an RNA Exosome-Independent Manner to Promote Cell Survival and Gene Expression during Stress. Cell reports, 31(10), 107754.
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7

Immunoprecipitation and Immunoblotting Assay

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Cells were harvested in lysis buffer (20 mm Tris-HCl pH 8, 137 mm NaCl, 2 mm EDTA and 1% NP-40) with protease inhibitor cocktail at 4 °C. Equal amounts of protein lysates were incubated with control IgG, anti-HA (ABM, Richmond, BC, Canada, G036), anti-Flag (Sigma, Allentown, PA, USA, F1804), or anti-ephrinB1 (R&D systems, AF473) at 4 °C overnight under mild agitation. Protein A/G-agarose beads (Santa Cruz Biotechnology, Santa Cruz, CA, USA) were then incubated for 1 h, followed by washing three times with lysis buffer. Immunoprecipitates and total protein lysates were separated by SDS–PAGE and immunoblotted with anti-HA-HRP (Roche, Billerica, MA, USA, 12013819001), anti-Flag-HRP (Sigma, A8592), anti-V5 (Invitrogen, Carlsbad, CA, USA, R961-25), anti-ephrinB1 (R&D Systems, af473) or anti-ephrinB (Santa Cruz Biotechnology C18, SC-910), anti-EphB2 (R&D Systems, AF467), anti-RhoGDI1 (Santa Cruz Biotechnology, SC-360) and anti-RhoA (Santa Cruz Biotechnology, SC-418), anti-Rac1 (Millipore, Billerica, MA, USA, 05-389), anti-Cdc42 (BD Bioscience, San Jose, CA, USA, 610929) and α-tubulin (Sigma, T6199).
Cho H.J., Hwang Y.S., Yoon J., Lee M., Lee H.G, & Daar I.O. (2017). EphrinB1 promotes cancer cell migration and invasion through the interaction with RhoGDI1. Oncogene, 37(7), 861-872.
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