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Anti v5 tag

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The Anti-V5-tag is a laboratory reagent used for the detection and purification of proteins tagged with the V5 epitope. The V5 epitope is a short peptide sequence that can be added to recombinant proteins, allowing for their identification and isolation using this antibody.

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Lab products found in correlation

Anti β actin, by Cell Signaling Technology (2 mentions) Anti wapl, by Thermo Fisher Scientific (2 mentions) Goat anti mouse hrp, by Jackson ImmunoResearch (1 mentions) Goat anti rabbit hrp, by Jackson ImmunoResearch (1 mentions) Anti gapdh, by Santa Cruz Biotechnology (1 mentions) Anti tubulin, by Abcam (1 mentions) Anti h2ax, by Merck Group (1 mentions) Anti h3k36me3, by Abcam (1 mentions) Anti rcc 1, by Santa Cruz Biotechnology (1 mentions) Anti p21, by Santa Cruz Biotechnology (1 mentions) Anti h3, by Abcam (1 mentions) Anti myc, by Abcam (1 mentions) Anti ha, by Fortrea (1 mentions) Odyssey blocking buffer, by LI COR (1 mentions) Anti β actin, by Abcam (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Infrared tagged secondary antibodies, by LI COR (1 mentions)

Spelling variants of this product

V5-tag (24 citations) Anti-V5 (21 citations) Rabbit anti-V5 tag (2 citations) Anti–V5-tag antibody (2 citations)

4 protocols using anti v5 tag

1

Western Blotting: Antibody Detection

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Western blotting was performed according to standard laboratory protocols. Antibodies used were: anti-H3K36me3 (Abcam, 9050; 1:1000), anti-H3 (Abcam, 1791; 1:5000), anti-HA (Covance, MMS-101P; 1:2000), anti-H2AX (Millipore 05-636; 1:5000) anti-Tubulin (Abcam, 7291; 1:5000), anti-RCC-1 (Santa Cruz, sc-55559; 1:2000), anti-p21 (Santa Cruz, sc-6246; 1:1000), anti-GAPDH (Santa Cruz, sc-365062; 1:1000), anti-V5-tag (Cell Signaling, 13202; 1:2000), anti-Myc (Abcam, 9106; 1:10000). Secondary antibodies used were: goat anti-mouse HRP (Jackson ImmunoResearch, 115-035-03 or Thermo Fisher Scientific, 31430; 1:5000), goat anti-rabbit HRP (Jackson ImmunoResearch, 111-035-003 or Thermo Fisher Scientific 31460; 1:5000). Uncropped scans of all blots are shown in Supplementary Fig. 12.
Skucha A., Ebner J., Schmöllerl J., Roth M., Eder T., César-Razquin A., Stukalov A., Vittori S., Muhar M., Lu B., Aichinger M., Jude J., Müller A.C., Győrffy B., Vakoc C.R., Valent P., Bennett K.L., Zuber J., Superti-Furga G, & Grebien F. (2018). MLL-fusion-driven leukemia requires SETD2 to safeguard genomic integrity. Nature Communications, 9, 1983.
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2

Western Blotting of RAG1-Deficient Cells

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Western blotting samples were prepared with short-term cultured RAG1-deficient primary pro-B cells, cycling RAG1-deficient v-Abl cells, and G1-arrested RAG1-deficient v-Abl cells with or without Wapl depletion. Western blotting experiments were performed according to published protocol with a few modifications36 (link). 10 million cells were harvested and lysed. Indicated antibodies (anti-Wapl, Thermo Fisher Scientific, #PA5–38024, 1:500; anti-V5-tag, #R960–25, 1:1000; anti-β-actin, Cell Signaling Technology, #3700, 1:3000) were used for the related western blotting experiments. For quantification and comparison of Wapl protein levels, the integrated density of Wapl and β-actin western blotting bands were calculated by Image J (version 1.42q) (Fig. 4b; Extended Data Fig. 6i). See Supplementary Figure 1 for uncropped scan blots with individual repeats.
Dai H.Q., Hu H., Lou J., Ye A.Y., Ba Z., Zhang X., Zhang Y., Zhao L., Yoon H.S., Chapdelaine-Williams A.M., Kyritsis N., Chen H., Johnson K., Lin S., Conte A., Casellas R., Lee C.S, & Alt F.W. (2021). Loop Extrusion Mediates Physiological IgH Locus Contraction For RAG Scanning. Nature, 590(7845), 338-343.
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3

Western Blotting of RAG1-Deficient Cells

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Western blotting samples were prepared with short-term cultured RAG1-deficient primary pro-B cells, cycling RAG1-deficient v-Abl cells, and G1-arrested RAG1-deficient v-Abl cells with or without Wapl depletion. Western blotting experiments were performed according to published protocol with a few modifications36 (link). 10 million cells were harvested and lysed. Indicated antibodies (anti-Wapl, Thermo Fisher Scientific, #PA5–38024, 1:500; anti-V5-tag, #R960–25, 1:1000; anti-β-actin, Cell Signaling Technology, #3700, 1:3000) were used for the related western blotting experiments. For quantification and comparison of Wapl protein levels, the integrated density of Wapl and β-actin western blotting bands were calculated by Image J (version 1.42q) (Fig. 4b; Extended Data Fig. 6i). See Supplementary Figure 1 for uncropped scan blots with individual repeats.
Dai H.Q., Hu H., Lou J., Ye A.Y., Ba Z., Zhang X., Zhang Y., Zhao L., Yoon H.S., Chapdelaine-Williams A.M., Kyritsis N., Chen H., Johnson K., Lin S., Conte A., Casellas R., Lee C.S, & Alt F.W. (2021). Loop Extrusion Mediates Physiological IgH Locus Contraction For RAG Scanning. Nature, 590(7845), 338-343.
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4

Western Blotting for NS5A Protein

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Cells were washed twice in PBS and lysed in Glasgow Lysis Buffer [GLB; 1 % (vol/vol) Triton X-100, 120 mM KCl, 30 mM NaCl, 5 mM MgCl2, 10 % (vol/vol) glycerol, 10 mM PIPES [piperazine-N,N′-bis(2-ethanesulfonic acid)]-NaOH, pH 7.2, with protease and phosphatase inhibitors], and clarified by centrifugation at 2800 g for 5 min at 4 °C. Protein concentration was measured for normalization by bicinchoninic acid assay (BCA, Pierce). Proteins were resolved on 7.5 % polyacrylamide gel before being transferred to polyvinylidene difluoride (PVDF) membrane. Membranes were blocked in 50 % (v/v) Odyssey blocking buffer (LI-COR) in Tris-buffered saline (TBS) and incubated in primary antibodies overnight at 4 ˚C and infra-red tagged secondary antibodies (LI-COR) at room temperature for 1 h. Primary antibodies used were anti-NS5A (sheep, 1 : 5000, [36 (link)]), anti-V5 tag (rabbit, 1 : 1000, Cell Signalling Technologies) and anti β-actin (mouse, 1 : 20 000, abcam). Secondary antibodies were anti-sheep, anti-rabbit (both 800 nm) and anti-mouse (680 nm), all used at 1 : 15 000. Membranes were imaged using a LI-COR Odyssey infra-red imaging system.
Kelly L., Badhan A., Roberts G.C., Mbisa J.L, & Harris M. (2017). Manipulation of both virus- and cell-specific factors is required for robust transient replication of a hepatitis C virus genotype 3a sub-genomic replicon. The Journal of General Virology, 98(10), 2495-2506.
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