V5 antibody

Manufactured by Merck Group

Sourced in Israel, Senegal

The V5-antibody is a laboratory reagent used for the detection and identification of proteins that have been engineered to contain the V5 epitope tag. The V5-antibody binds specifically to the V5 tag, allowing for the visualization and purification of tagged proteins in various experimental procedures.

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Lab products found in correlation

β actin, by Merck Group (2 mentions) N cadherin antibody, by Cell Signaling Technology (1 mentions) Mmp 9 antibody, by Cell Signaling Technology (1 mentions) Snail antibody, by Cell Signaling Technology (1 mentions) Vimentin antibody, by Cell Signaling Technology (1 mentions) Anti flag beads, by Merck Group (1 mentions) V5 peptide, by Merck Group (1 mentions) Ni nta bead, by Qiagen (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) Anti ha antibody ha 11, by Fortrea (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Phosstop, by Roche (1 mentions)

Close spelling variants of this product

Anti-V5 antibody (17 citations) Mouse monoclonal anti-V5 antibody (3 citations) Anti-V5 agarose affinity gel antibody (3 citations) Monoclonal anti-V5 antibody (3 citations) Flag or V5 antibody-conjugated beads (2 citations) Anti-V5 antibody conjugated agarose beads (2 citations) Anti-V5 tag antibody (2 citations) Mouse anti-V5 antibody (2 citations) Rabbit anti-V5 antibody (2 citations) V5-tag antibody (2 citations)

4 protocols using v5 antibody

Western Blot Antibody Profiling

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Antibodies against Nudt2 (#10484-1-AP, dilution 1:1000, Proteintech, Biotest, Kfar Saba, Israel), β-Actin (#A1978, dilution 1:10,000, Sigma-Aldrich, Jerusalem, Israel), V5-antibody (#v8012, dilution 1:2000, Sigma Aldrich), vimentin antibody (#5741T, dilution 1:2000, Cell Signaling, Jerusalem, Israel), N cadherin antibody (#13116, dilution 1:2000, Cell Signaling, Jerusalem, Israel), MMP9 antibody (#13667, dilution 1:2000, Cell Signaling, Jerusalem, Israel), and Snail antibody (#3879, dilution 1:2000, Cell Signaling, Jerusalem, Israel) were used.

Hidmi S., Nechushtan H., Razin E, & Tshori S. (2023). Role of Nudt2 in Anchorage-Independent Growth and Cell Migration of Human Melanoma. International Journal of Molecular Sciences, 24(13), 10513.

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Immunoprecipitation of cell surface receptors

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A detailed experimental procedure is described in the supplement. In brief, intact 293T cells on ice were incubated with cold FLAG-AP-NDP conditioned medium, or V5-antibody (AbD Serotec) in cold medium, washed, and lysed. FLAG-AP-NDP or V5-antibody bound to the receptor complex at the cell surface was isolated using anti-FLAG beads (Sigma) or ProteinA/G beads (Pierce), respectively. Samples were analysed by immunoblot.

Lai M.B., Zhang C., Shi J., Johnson V., Khandan L., McVey J., Klymkowsky M.W., Chen Z, & Junge H.J. (2017). TSPAN12 is a Norrin Co-Receptor that Amplifies Frizzled4 Ligand Selectivity and Signaling. Cell reports, 19(13), 2809-2822.

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OLIG2 Protein Purification and Characterization

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OLIG2-V5-HIS cDNA was transiently transfected into COS-7 cells using the pcDNA3.1 vector. Cells were lysed in hypotonic lysis buffer (50 mM Tris-HCl at pH 7.5, 0.2% [v/v] NP-40, 5 mM EDTA) and then high salt buffer (final concentration: 10 mM HEPES, 420 mM NaCl, 0.2 mM EDTA). OLIG2 protein was then purified from cellular lysates by immunoprecipiation with V5 antibody (Sigma), V5 peptide (Sigma) elution, affinity purification with Ni-NTA beads (Qiagen), and elution in 200 mM imidazole and Buffer A (50 mM Tris at pH 7.5, 150 mM KCl, 5 mM MgCl₂, 10% [v/v] glycerol, 0.1% [v/v] NP40, and protease inhibitors).

Edwards A.L., Meijer D.H., Guerra R.M., Molenaar R.J., Alberta J.A., Bernal F., Bird G.H., Stiles C.D, & Walensky L.D. (2016). Challenges in Targeting a Basic Helix–Loop–Helix Transcription Factor with Hydrocarbon-Stapled Peptides. ACS chemical biology, 11(11), 3146-3153.

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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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