V5-Tag antibody | SV5-Pk1
Mouse anti V5-Tag antibody, clone SV5-Pk1 (MCA1360G) used for the evaluation of V5 tagged cif transfectants by western blotting
Image caption:
Cif increases ERK MAPK phosphorylation in a manner dependent on its deamidase activity but independent of CRL inhibition. (A,B) HEK293T cells were transfected with the indicated expression plasmids for two days, (B) and treated with 1 μM MLN4924 for the last 24 hours. Pre-cleared cell lysates were then subjected to Western blotting analysis with the indicated antibodies. (C) HEK293T cells were transfected for two days with V5-Cif, as indicated. Cells were then serum-starved for 3 hours, followed by cell lysis and Western blot analysis with the indicated antibodies. The phospho-p70 S6K1 Western blot served as a positive control for the effect of serum starvation. As expected, growth factor withdrawal resulted in reduced p70 S6K1 phosphorylation. It was also noted that Cif expression had an inhibitory effect on p70 S6K1 phosphorylation both in the presence and absence of serum. (D) Cells were transfected with the indicated expression plasmids. For V5-Cif C156S expression, increasing amounts were transfected whereby the lowest amount equaled that of the wild type V5-Cif expression plasmid. Cell lysates were analysed by Western blotting using the indicated antibodies. (E) Tetracycline-inducible dominant negative Ubc12 HEK293 cells were transfected with FLAG-Cif expression plasmid for two days. Cells were then either treated with 1 μM tetracycline to induce dnUbc12 expression for the last 24 hours or treated with 1 μM MLN4924 for the last 24 hours. Cell lysates were then analysed by Western blotting using the indicated antibodies.
From: Ng MY, Wang M, Casey PJ, Gan Y-H, Hagen T (2017)
Activation of MAPK/ERK signaling by Burkholderia pseudomallei cycle inhibiting factor (Cif).
PLoS ONE 12(2): e0171464.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5-Tag antibody, clone SV5-Pk1 (MCA1360G) used for the evaluation of V5 tagged cif transfectants by western blotting
Image caption:
Cif regulates the expression or activity of apoptosis related proteins.
(A) Cells were co-transfected with FLAG-BimEL and V5-Cif, MEK-DD or empty vector, or treated with 10 μM U0126 for the last 6 hours. Cell lysates were then subjected to Western blotting using the indicated antibodies. (B) Cells were co-transfected with FLAG-BimEL and V5-Cif, MEK-DD or empty vector and treated with 10 μM U0126 for the last 6 hours, as indicated, followed by Western blotting using the indicated antibodies. (C) Cells were transfected with FLAG-Cif, MEK-DD or empty vector and treated with 10 μM U0126 for the last 6 hours and with 1 μM MLN4924 for the last 24 hours, as indicated, followed by Western blotting using the indicated antibodies.
From: Ng MY, Wang M, Casey PJ, Gan Y-H, Hagen T (2017)
Activation of MAPK/ERK signaling by Burkholderia pseudomallei cycle inhibiting factor (Cif).
PLoS ONE 12(2): e0171464
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5-Tag antibody, clone SV5-Pk1 (MCA1360G) used for the evaluation of V5 tagged cif transfectants by western blotting
Image caption:
Cif activates MAPK/ERK signaling in a manner independent of MAPK phosphatases.
Cells were transfected with V5-Cif or B-Raf-V600E and treated with 10 μM U0126 for the last 5 to 120 minutes, followed by Western blotting of the cell lysates using the indicated antibodies.
From: Ng MY, Wang M, Casey PJ, Gan Y-H, Hagen T (2017)
Activation of MAPK/ERK signaling by Burkholderia pseudomallei cycle inhibiting factor (Cif).
PLoS ONE 12(2): e0171464.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5-Tag antibody, clone SV5-Pk1 (MCA1360G) used for the evaluation of V5 tagged cif transfectants by western blotting
Image caption:
Cif likely activates MAPK/ERK signaling at the level of the Grb2-SOS1 complex.
(A-C, E-F) Cells were transfected with the indicated expression plasmids for two days, and then treated with (A) 10 μM BAY 43–9006 or 0.1% DMSO for the last 6 hours or (E) 1 μM MLN4924 for the last 24 hours, followed by Western blotting of the cell lysates using the indicated antibodies. (D) Cells were transfected with the indicated expression plasmids for two days. The cells were then incubated for 6.5 hours in serum free medium, followed by re-addition of serum for 30 min, where indicated. The cell lysates were then analysed by Western blotting using the indicated antibodies.
From: Ng MY, Wang M, Casey PJ, Gan Y-H, Hagen T (2017)
Activation of MAPK/ERK signaling by Burkholderia pseudomallei cycle inhibiting factor (Cif).
PLoS ONE 12(2): e0171464.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5-Tag antibody, clone SV5-Pk1 (MCA1360G) used for the evaluation of V5 tagged cif transfectants by western blotting
Image caption:
Cif expression regulates the CDC25-H and proline-rich domains in SOS1.(A,B) HEK293T cells were transfected with the indicated expression plasmids for two days, followed by FLAG immunoprecipitation of the cell lysates using FLAG-agarose and Western blotting of the immunoprecipitates and aliquots of the cell lysates using the indicated antibodies. (C) All cells were transfected with FLAG-SOS1 as well as V5-Cif or empty vector, as indicated, for two days. Cells were then lysed in hypotonic lysis buffer (25 mM Tris-HCL, 2 mM EDTA, 2 mM EGTA, 0.1% β-Mercaptoethanol, Roche protease inhibitor cocktail, pH 7.5) and cell lysates subjected to freeze-thawing at -80°C. The cytosolic fraction was separated from the remaining cellular compartments (membranes and nuclear fraction) through centrifugation. The proteins in the cytosolic supernatant and the pellet were denatured using SDS loading buffer and analysed using Western blotting with the indicated antibodies. Equal corresponding amounts of cytosol and pellet were loaded. GAPDH served as a control for the cytosolic fraction and calnexin as a control for the membrane fraction. Glut1 (55 kDa) served as an additional control for the membrane fraction, as the higher molecular weight, glycosylated Glut1 species can only be detected in the membrane fraction. (D) Cells were transfected with the indicated FLAG-mSOS1 truncation constructs for two days, followed by Western blotting using the indicated antibodies. The bottom FLAG blot in the Western blot panel was obtained from running a duplicate set of lysates through another SDS-PAGE gel of a lower resolving gel percentage for a longer time to increase the resolving power.
From: Ng MY, Wang M, Casey PJ, Gan Y-H, Hagen T (2017)
Activation of MAPK/ERK signaling by Burkholderia pseudomallei cycle inhibiting factor (Cif).
PLoS ONE 12(2): e0171464.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for the detection of V5 tagged p53-binding protein-1 by western blotting
Image caption:
hMSL2 mediates modification of 53BP1, hMSL1 and hMOF. (A) Alignment of the two peptide sequences in 53BP1 (subject) that are reported as similar to the sequence containing H2BK34 (query), and schematic showing the M-domain of 53BP1. Lysine 1568 (white circle) lies within the second Tudor domain and lysine 1690 (grey circle) lies within the nuclear localization sequence (NLS). OD represents the oligomerization domain. Also shown is lysine 1273 (black circle) reported to be ubiquitylated by RAD18. (B) Immunoblot analysis of U2OS cells that were transfected with both His-ubiquitin and HA2F-hMSL2, together with either V5-53BP1-M-domain wild-type or point mutant constructs. Mock cells were not transfected with any of the plasmids. (C and D) Immunoblot analysis of U2OS cells, with transfection of His-ubiquitin and with/without transfection of HA2F-hMSL2. Cells were treated with 10 Gy of IR as indicated and harvested 15 minutes after IR. V5-Mdomain, endogenous hMSL1 and endogenous hMOF are indicated with an arrowhead. Modified proteins are indicated with an open arrowhead.
From: Lai Z, Moravcová S, Canitrot Y, Andrzejewski LP, Walshe DM,et al. (2013)
Msl2 Is a Novel Component of the Vertebrate DNA Damage Response.
PLoS ONE 8(7): e68549.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5-TAG antibody, clone SV5-Pk1 used for immunofluorecence of tranfected RAW264.7 cells.
Image caption:
Subcellular localisation of Hsa_aTRACP. Immunofluoresence staining of RAW264.7 cells transfected with a Hsa_aTRACP-V5 using the Alexa488 goat anti-mouse antibody (Invitrogen) in combination with the mouse anti-V5 IgG2a (Bio-Rad) and visualised using Alexa594 Phalloidin stain (Invitrogen). DNA was stained with DAPI (Roche). Evident is the diffuse cytoplasmic distribution of Hsa_aTRACP.
From: Hadler KS, Huber T, Cassady AI, Weber J, Robinson J, Burrows A, Kelly G, Guddat LW, Hume DA, Schenk G, Flanagan JU.
Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?
BMC Res Notes. 2008 Sep 4;1:78.
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Mouse anti V5 Tag antibody, clone SV5-Pk1used for immunoprecipitation of V5 tagged RNF11 protein
Image caption:
Dynamic associations of RNF11 with both A20 and Itch in primary neurons. N2A cells transduced with V5-RNF11 lentivirus (N2A V5-RNF11) and transfected with FLAG-A20 were harvested for immunoprecipitation (IP) with V5 antibody (A) or harvested for IP with FLAG antibody (B). Proteins were resolved by SDS-PAGE and immunoblotted with anti-A20 and RNF11. In parallel, pull-down assays with V5 antibody (C) or with Itch antibody (D) from N2A V5-RNF11 cell lysates were resolved by SDS-PAGE. Immunoprecipitates and lysates were immunoblotted with anti-Itch and RNF11. (E) and (H) Murine primary cortical neurons were stimulated with 10 ng/ml TNF-α for 0 or 30 minutes and harvested for IP with RNF11 antibody. Control IP experiments were performed with antibody omitted. Proteins were resolved by SDS-PAGE and immunoblotted with anti-A20, Itch, RNF11 and actin. (F), (G), (I) and (J) ImageJ software was used to quantify the densitometry of the immunoprecipitated bands relative to the 0-minutes time point. Each input sample’s immunoreactivity was used as a loading control. All IPs are representative of at least three independent experiments. *P < 0.05.
From: Pranski EL, Dalal NV, Herskowitz JH, Orr AL, Roesch LA, Fritz JJ, Heilman C, Lah JJ, Levey AI, Betarbet RS.
Neuronal RING finger protein 11 (RNF11) regulates canonical NF-κB signaling.
J Neuroinflammation. 2012 Apr 16;9:67.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 Tag antibody, clone SV5-Pk1used for immunoprecipitation of V5 tagged RNF11 protein
Image caption:
Myristoylation mutant of RNF11 is unable to associate with Itch. SH-SY5Y shRNA-RNF11 cells were transfected with shRNA-resistant RNF11 constructs or vector. Coimmunoprecipitation experiments using V5 antibody were performed 24 hours after transfection. Immunoprecipitates and lysates were resolved by SDS-PAGE and immunoblotted with anti-A20, Itch, RNF11 or actin. Blots are representative of three independent experiments.
From: Pranski EL, Dalal NV, Herskowitz JH, Orr AL, Roesch LA, Fritz JJ, Heilman C, Lah JJ, Levey AI, Betarbet RS.
Neuronal RING finger protein 11 (RNF11) regulates canonical NF-κB signaling.
J Neuroinflammation. 2012 Apr 16;9:67.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for detection of V5 tagged REDD1 protein by western blotting.
Image caption:
Negative feedback regulation of REDD1. (A) REDD1-V5 pcDNA3 (0.4 μg) was transfected in HEK293 cells for 3 days followed by cell lysis and detection of endogenous REDD1 proteins by Western blotting. (B) HEK293 cells with and without the transfection of REDD1-V5 pcDNA3 (0.15 μg) were treated with 20 nM rapamycin for 4 or 36 hours followed by cell lysis. (C) MEF TSC2+/+ and TSC2−/− cells were treated with rapamycin (40 nM) or PP242 (2 μM) for 24 hours before cell lysis. Detection of V5 tag, REDD1, α-tubulin, phosphorylated and total S6 Kinase 1 was performed by Western blotting as described in Materials and methods.
From: Tan CY, Hagen T (2013)
mTORC1 Dependent Regulation of REDD1 Protein Stability.
PLoS ONE 8(5): e63970.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for detection of V5 tagged REDD1 protein by western blotting.
Image caption:
REDD1 is not regulated by Cullin E3 Ubiquitin ligases. (A,B) Untransfected (A) or REDD1-V5 pcDNA3 (0.3 μg) transfected (B) HEK293 cells stably expressing tetracycline inducible dnUbc12-HA were induced with 1 μg/ml tetracycline for 24 hours (A,B) or treated with 3 μM MLN4924 (A) or 20 μM MG-132 (A,B) for 8 hours followed by cell lysis. (C,D) Untransfected HEK293 (C) or HEK293 transfected with REDD1-V5 pcDNA3 (0.3 μg) (D) were pre-treated with 3 μM MLN4924 followed by cycloheximide (40 μM) treatment and cell lysis at the indicated time points. (E) HEK293 cells stably expressing tetracycline inducible dnUbc12-HA were induced with 1 μg/ml tetracycline for 24 hours followed by cycloheximide (40 μM) treatment and cell lysis at the indicated time points.
From: Tan CY, Hagen T (2013)
mTORC1 Dependent Regulation of REDD1 Protein Stability.
PLoS ONE 8(5): e63970.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for detection of V5 tagged REDD1 protein by western blotting.
Image caption:
REDD1 is not degraded by Cul4a or phosphorylated by GSK3β at Thr 23 and Thr25. (A) HEK293 cells were transfected with empty vector or tetracycline inducible dnCul4a-V5 pcDNA4/TO (1 μg) and Cul4A-V5 pcDNA3 (0.03 μg) followed by tetracycline (1 μg/ml) induction for 24 hours and cell lysis. (B) HEK293 cells were transfected with 0.5 μg Cul4a-V5 pcDNA3 for 15 hours followed by transfection of 20 nM control or Cul4a siRNAs to determine siRNAs efficiency. (C) HEK293 cells were transfected with 20 nM control or Cul4a siRNAs for 3 days followed by cell lysis. (D) REDD1-V5 pcDNA3 wild type, T23A T25A or T23D T25D plasmids (0.4 μg) were transfected in HEK293 cells for 3 days and treated with 20 μM MG-132 for 6 hours followed by cell lysis. (E) HEK293 cells were treated with 30 mM LiCl or GSK3 inhibitor IX (5 μM or 10 μM) for 20 hours followed by cell lysis. (F) HEK293 cells were co-transfected with 0.2 μg REDD1-V5 pcDNA3 and 0.3 μg GSK3β pcDNA3 or empty pcDNA3 for 3 days followed by MG-132 (20 μM) treatment for 6 hours followed by cell lysis. (G) HEK293 cells were transfected with 3 μg FLAG-REDD1 or FLAG-FRAT1 for 3 days followed by cell lysis and FLAG immunoprecipitation. In vitro phosphorylation of REDD1 and FRAT1 was carried out as described in Materials and Methods..
From: Tan CY, Hagen T (2013)
mTORC1 Dependent Regulation of REDD1 Protein Stability.
PLoS ONE 8(5): e63970.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for detection of V5 tagged podocin protein by western blotting
Image caption:
The podocin short isoform is retained in the ER and is found in the detergent resistant membrane fraction. A) PCR with podocin specific primers yields products for both isoforms from a human kidney cDNA library. B) Immunofluorescence staining of the canonical and the short isoform in Hela cells transfected with the corresponding constructs show that only the canonical isoform reaches the plasma membrane (arrowhead in the enlarged part of the image). The short isoform is retained in the endoplasmic reticulum. Scale bar = 10 μm. C) DRM association of both podocin isoforms. HEK293T cells expressing the respective V5-tagged podocin isoform were lysed in 1% TX-100 on ice and subjected to sucrose density gradient centrifugation. Fractions 1–7 were collected from the top and analyzed by Western blot. Both isoforms fractionate into the DRMs (fractions 1 and 2, as identified by flotillin staining). Antibodies against the transferrin receptor (TfR) and Flotillin-2 were used as markers for the Triton soluble and insoluble fractions, respectively.
From: Völker LA, Schurek EM, Rinschen MM, Tax J, Schutte BA, Lamkemeyer T, Ungrue D, Schermer B, Benzing T, Höhne M.
Characterization of a short isoform of the kidney protein podocin in human kidney.
BMC Nephrol. 2013 May 6;14:102.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for detection of V5 tagged podocin protein by western blotting
Image caption:
The podocin short isoform interacts with known podocyte proteins. CD2AP, TRPC6, neprin and NEPH1 co-precipitate with both podocin isoforms (FL, full length (canoncical isoform); SI, short isoform). FLAG- and V5-tagged proteins were expressed in HEK293T cells and precipitated with anti-FLAG antibody as indicated. Western blot analysis was performed with a V5 specific antibody. Expression levels of FLAG.podocin constructs in the lysates are shown below.
From: Völker LA, Schurek EM, Rinschen MM, Tax J, Schutte BA, Lamkemeyer T, Ungrue D, Schermer B, Benzing T, Höhne M.
Characterization of a short isoform of the kidney protein podocin in human kidney.
BMC Nephrol. 2013 May 6;14:102.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for detection of V5 tagged podocin protein by western blotting
Image caption:
The podocin short isoform is N-glycosylated. A) PNGase-F treatment removes the double band from the short isoform in DRM fraction 7. Lysates from Figure 3 were subjected to treatment with PNGase-F and immunoblotted and detected with anti-V5 antibody. B) N to S mutation of the N-glycosylation consensus motif completely abrogates the formation of a double band. The asparagine at position 287 corresponds to amino acid 355 in the full-length protein. HEK293T cells were transfected with V5-tagged Podocin (short isoform or short isoform N287S, respectively) and lysates were immunoblotted and detected with anti-V5 antibody.
From: Völker LA, Schurek EM, Rinschen MM, Tax J, Schutte BA, Lamkemeyer T, Ungrue D, Schermer B, Benzing T, Höhne M.
Characterization of a short isoform of the kidney protein podocin in human kidney.
BMC Nephrol. 2013 May 6;14:102.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for the detection of V5 tagged NFAT5 protein by western blotting
Image caption:
Effect of knock down of 14‐3‐3‐β and/or ‐ε on protein abundance of NFAT5. (A) Knock down of 14‐3‐3‐β and/or ‐ε reduces NFAT5 protein abundance. siRNAs against 14‐3‐3‐β and/or ‐ε were transfected for 3 days into HEK293 cells incubated at 300 mosmol/kg, then the medium was changed, keeping the osmolality at 300 or increasing it to 500 mosmol/kg for 8 h by adding NaCl. Upper panel is a representative Western blot. The siRNAs singly and in combination reduce NFAT5 protein abundance (mean ± SEM, n = 3, *P<0.05). (B) Time course of the effect of 14‐3‐3‐β and ‐ε in combination. As in (A) except that NFAT5 protein was measured just before NaCl was increased (zero time) and after that at the intervals that are shown. Upper panel is a representative Western blot (Mean ± SEM, *P<0.05, n = 3). (C) Lack of effect of 14‐3‐3‐β and/or ‐ε separately or combined on NFAT5 mRNA abundance. As in (A) except that NFAT5 mRNA was measured 16 h after NaCl was increased (P>0.05, n = 3). (D–F) siRNA‐mediated knockdown of 14‐3‐3‐β and ‐ε in combination increases degradation of NFAT5 protein. siRNAs against 14‐3‐3‐β and ‐ε were transfected for 3 days into HEK293 cells incubated at 300 mosmol/kg. (D) One hundred μg/mL cycloheximide (CHX) or vehicle (DMSO control) was added for 1 h before changing to otherwise identical media kept at 300 mosmol/kg or increased to 500 mosmol/kg by adding NaCl. Media contained CHX or DMSO. NFAT5 protein was measured by Western blot at the start and end of the 8 h increase in NaCl, and the difference (Δ) was calculated. (*P<0.05, n = 3). (E and F) Measurement of the rate of NFAT5 degradation by cycloheximide chase. HEK293 cells were preincubated for 7 h at 300 or 500 mosmol/kg, then 100 μg/mL cycloheximide was added for 1 h. Cells maintained in cycloheximide were harvested at the intervals shown. (*P<0.05, n = 3–4). (G) Lack of coimmunoprecipitation of 14‐3‐3‐β and ‐ε with NFAT5. NFAT5‐V5 was immunoprecipitated from HEK293 cells, then the immunoprecipitates were immunoblotted for the proteins shown. CDK5 and HSP90 coimmunoprecipitate with NFAT5‐V5, but 14‐3‐3‐β and ‐ε do not.
From: Izumi Y, Burg MB, Ferraris JD.
14-3-3-β and -ε contribute to activation of the osmoprotective transcription factor NFAT5 by increasing its protein abundance and its transactivating activity.
Physiol Rep. 2014 Apr 22;2(4):e12000.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5.Pk1 used for the detection of V5 tagged podocin by immunofluorescence
Image caption:
Podocin localizes to endosomal vesicles. Immunofluorescence for transiently expressed, V5- (a–c, e) or Flag-tagged (d) podocin using anti-V5 or anti-Flag antibody in HeLa cells. Costainings of endogenous calnexin (a), endogenous golgin-97 (b), endogenous EEA1 (c), Lysotracker Red (d) and eGfp-tagged and transiently expressed CD63 (e) as markers for the endoplasmatic reticulum, Golgi apparatus, early endosomes, acidic organelles and late endosomes respectively, displayed that podocin localizes to the endosomal compartment. Analogously to HeLa cells, transiently expressed V5-tagged podocin colocalizes with eGFP tagged CD63/LAMP3 in cultured human podocytes (f).
From: Gödel M, Ostendorf BN, Baumer J, Weber K, Huber TB (2013)
A Novel Domain Regulating Degradation of the Glomerular Slit Diaphragm Protein Podocin in Cell Culture Systems.
PLoS ONE 8(2): e57078.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for the detection of V5 tagged Rho GTPase-activating protein 28 protein by western blotting and immunofluorescence
Image caption:
Arhgap28-V5 inhibits RhoA activation and stress fiber formation in SaOS-2 cells. SaOS-2 cells were transfected with empty vector or Arhgap28-V5. A. The expression of Arhgap28-V5 was confirmed by western blotting using an antibody to V5. B. Effect of Arhgap28-V5 expression on the basal activity of RhoA (n = 5), Rac1 (n = 3) and Cdc42 (n = 3). Bars show SEM. * indicates significant difference found, p<0.05. C–D. F-actin in cells expressing Arhgap28-V5 (C) and Arhgap28R425A-V5 (D) was visualized by fluorescence microscopy using anti-V5 antibodies and Atto 488-conjugated phalloidin (representative images from 3 independent transfections). Arrows point to membrane ruffling and F-actin protrusions. Bars = 25 μm.
From: Yeung C-YC, Taylor SH, Garva R, Holmes DF, Zeef LA, et al. (2014)
Arhgap28 Is a RhoGAP that Inactivates RhoA and Downregulates Stress Fibers.
PLoS ONE 9(9): e107036.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 used for the detection of V5 tagged HIVA peptide by western blotting
Image caption:
Construction of the BCG.HIVACAT vaccine strain. (A) A synthetic GC-rich HIVA gene was fused to the region encoding the 19-kDa lipoprotein signal sequence and inserted into the episomal pJH222 E. coli-mycobacterium shuttle plasmid. This plasmid contains kanamycin resistance (aph) and complementing lysA genes and an E. coli origin of replication (oriE). In addition, pJH222 contained the mycobacterial origin of replication (oriM). The BALB/c mouse T-cell and MAb Pk epitopes used in this work are depicted. P α-Ag, M. tuberculosis α-antigen promoter; PHSP60, heat shock protein 60 gene promoter. The aph gene was removed by SpeI digestion and the lacO sequence was inserted and transformed into E. coli DH1lacdapD strain. (B) Immunodot of BCG.HIVACAT lysates. Dot 1: BCG wild type (negative control); Dot 2, 3, 4 and 5: clone 3, clone 7, clone 9 and clone 10 of BCG.HIVACAT; Dot 6: BCG.HIVA222 (positive control). HIVA peptide was detected using the anti-Pk MAb followed by horseradish peroxidase-Goat-anti-Mouse and enhanced chemiluminescence (ECL) detection. (C) In vivo plasmid stability of BCG.HIVACAT harboring pJH222.HIVACAT. Mice were injected s.c. with 105 cfu of BCG.HIVACAT and boosted i.m. with 106 pfu of MVA.HIVA, spleens were homogenized 20 weeks after BCG inoculation and the recovered rBCG colonies were tested for the presence of the HIVA DNA coding sequence by PCR. Lanes 1 to 6: Six rBCG colonies were recovered in the non-lysine supplemented plate; lane 7: Molecular weight marker; lane 8: Plasmid DNA positive control; lane 9: Distilled water (negative control).
From: Saubi N, Mbewe-Mvula A, Gea-Mallorqui E, Rosario M, Gatell JM, et al. (2012)
Pre-Clinical Development of BCG.HIVACAT, an Antibiotic-Free Selection Strain, for HIV-TB Pediatric Vaccine Vectored by Lysine Auxotroph of BCG.
PLoS ONE 7(8): e42559.
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Mouse anti V5 tag antibody, clone SV5-Pk1 used for the detection of V5 tagged WEEV_nsP3 protein by western blotting and immunofluorescence
Image caption:
WEEV nsP3 interaction with host IKKβ. A) U87MGs were transfected in a 6-well plate with 5 μg of pUC19 and WEEV_nsP3_HA for 24 hours. Cell lysates were resolved using SDS-PAGE and subsequently immunoblotted with V5 antibody and β-actin served as a loading control. B) U87MGs were transfected with WEEV_nsP3_V5; cells were fixed after 24 hours and stained with antibodies against the endogenous IKKβ and the V5 tag. Cells were incubated with appropriate secondary Alexa Fluor antibodies and the nuclei stained with DAPI. Co-localization of IKKβ with WEEV_nsP3_V5 (yellow) was observed as shown by the arrows. B) Panels E–H serve as an example of transfected cells in a given field of view that show co-localization of IKKβ and WEEV_nsP3_V5 24 hours post transfection. Panels I-L represent magnified images of other cells showing co-localization of IKKβ and WEEV_nsP3_V5. Panel M is a magnified image of panel L. The co-localization was confirmed by Z-stack analysis. Co-localization was calculated to be approximately in 61% of cells (163 cells were counted of which 44% demonstrated expression of nsP3. Of those cells that expressed nsP3, 61% showed co-localization of both proteins). Images were taken using Nikon Eclipse TE2000-U at 60× magnification and are representative of 2 independent experiments.
From: Amaya M, Voss K, Sampey G, Senina S, de la Fuente C, et al. (2014)
The Role of IKKβ in Venezuelan Equine Encephalitis Virus Infection.
PLoS ONE 9(2): e86745.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Mouse anti V5 tag antibody, clone SV5-Pk1 (MCA1360) used to bind the SV5 tag on recombinant protein fragments by immunoblotting.
Image caption:
Identification of the motif of Sgo1 required for binding of the condensin complex.
Mapping of the binding sites of Sgo1 to the condensin complex using a peptide array. A1-H5: Sgo1 peptides, starting from position one, 15 aa, four aa overlap. H8 –H20: tags for antibody controls. Binding of the condensin complex with peptides A10, A11, A12 (amino acids from 37 to 59) and B16, B17, B18 (amino acids from 141 to 163) was considered as positive and validated in a secondary screen (S1A and S1B Fig).
From: Yahya G, Wu Y, Peplowska K, Röhrl J, Soh Y-M, Bürmann F, et al.. (2020)
Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast.
PLoS Genet 16(8): e1008569.
doi: 10.1371/journal.pgen.1008569
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Mouse anti SV5 tag antibody, clone SV5-Pk1 (MCA1360) used to identify V5 tagged proteins in lysates by western blotting.
Image caption:
The extensive interface between INTS13 and INTS14 requires several mutations for disruption.
i, j Coprecipitation experiments from HEK293T cells expressing patch double mutants in V5-SBP-INTS13 i or INTS14 j with the corresponding λN-HA-tagged binding partner. V5-SBP-MBP and the wt proteins were used as negative and positive controls, respectively. Inputs (αV5-blots 1%, αHA-blots 0.5%) and bound fractions (αV5-blots 4%, αHA-blots 20% and 10%) were analyzed by Western blotting.
From: Sabath K, Stäubli ML, Marti S, Leitner A, Moes M, Jonas S.
INTS10-INTS13-INTS14 form a functional module of Integrator that binds nucleic acids and the cleavage module.
Nat Commun. 2020 Jul 9;11(1):3422.
doi: 10.1038/s41467-020-17232-2.
This image is from an open access article distributed under terms of a Creative Commons Attribution License.
Mouse anti V5-tag antibody, clone SV5-Pk1 (MCA1360) used to evaluate BMH1 expression in Drosophila whole cell extracts by immunoprecipitation and western blotting.
Image caption:
Suppression of fork collapse in exo1–23D rad53Δ mutants is independent of the 14-3-3 proteins. (A) Analysis of Bmh1-PK and Exo1-MYC interaction in EXO1-MYC BMH1-PK and EXO1-MYC BMH1-PK rad53Δ strains. G1-blocked cells were released into YPD medium containing or not 0.2M HU for 90 min. Cells were harvested and proteins were pulled down with anti-MYC antibody, and a fraction of the Whole Cell Extract (WCE), and the co-immunoprecipitated proteins (IP) are shown in the immunoblot. Exo1-MYC was detected with anti-MYC antibody and Bmh1-PK with anti-PK antibody. (B) Co-immunoprecipitation assay of Exo1-MYC as described in (A). Proteins were pulled down with anti-PK antibody. Analysis of Phostag-SDS page from WCE and IP proteins are shown in the lower panel. (C) Immunoblot of a co-immunoprecipitation assay of an EXO1-MYC BMH1-PK, an exo1–23D-MYC BMH1-PK and an exo1–23A-MYC BMH1-PK strains in HU as in (A) is shown in the upper panels. Strains that lacked MYC-tagged Exo1 were used for the co-immunoprecipitation assay shown in the lower panels (EXO1+BMH1-PK, exo1–23D BMH1-PK and exo1–23A BMH1-PK). A fraction of the supernatant (Sup.) is also shown in the immunoblot. (D) Analysis of replication intermediates by 2D gel electrophoresis at the ARS305 in rad53Δ exo1–23D bmh2Δ bmh1–266 strains in the presence of 0.2 M HU. The graphs show the quantification analysis of replication bubbles.
From: Morafraile EC, Bugallo A, Carreira R, Fernández M, Martín-Castellanos C, Blanco MG, Segurado M.
Exo1 phosphorylation inhibits exonuclease activity and prevents fork collapse in rad53 mutants independently of the 14-3-3 proteins.
Nucleic Acids Res. 2020 Apr 6;48(6):3053-70.
doi: 10.1093/nar/gkaa054.
This image is from an open access article distributed under terms of a Creative Commons Attribution License.
Dylight 550 conjugated Mouse anti V5-tag antibody, clone SV5-Pk1 (MCA1360D550GA) used to detect Erm-V5 tagged protein in Drosophila by immunofluorescence.
Image caption:
Lola regulates the progression of the temporal cascade. g–g”’ In lola-RNAi clones (VDRC 101925), Erm-V5 (red) is activated in the 3rd or 4th NB marked by Dpn(blue) (in 16 out of 16 clones), whereas in wild-type regions, Erm-V5 is activated in the 2nd or 3rd NB. h–h”’ In lola-RNAi clones (VDRC 101925), the activation of Ey (red) is observable in the 4th or 5th NB marked by Dpn (blue) (in 19 out of 19 clones), while wild-type Ey expression starts in the 2nd or 3rd NB. i–i”’ In lola-RNAi clones (VDRC 101925), Slp2 (red) is activated in the 7th to 9th NB marked by Dpn (blue) (in 24 out of 24 clones), whereas in wild-type part of the brains, Slp2 is activated in the 4th or 5th NB. j A schematic showing the function of Lola in regulating the temporal cascade. Loss of Lola causes slowing down of the temporal progression. In wild type, only seven NBs were shown because later TTFs were not examined. Scale bars: 20μm.
From: Zhu H, Zhao SD, Ray A, Zhang Y, Li X.
A comprehensive temporal patterning gene network in Drosophila medulla neuroblasts revealed by single-cell RNA sequencing.
Nat Commun. 2022 Mar 10;13(1):1247.
doi: 10.1038/s41467-022-28915-3.
This image is from an open access article distributed under terms of a Creative Commons Attribution License.
Filter by Application:
E WB IF IP IB ResetMouse anti V5-Tag
- Product Type
- Monoclonal Antibody
- Clone
- SV5-Pk1
- Isotype
- IgG2a
- Specificity
- V5-Tag
Antibody Quality and Performance Guarantee
| Mouse anti V5-Tag, clone SV5-Pk1 recognizes the sequence, IPNPLLGLD, present on the P/V proteins of the paramyxovirus, SV5 (Dunn et al.1999). Clone SV5-Pk1 is used to detect recombinant proteins, some of which include transmembrane and secreted proteins, that have labeled with tags containing this sequence (Randall et al.1993 and Zhao et al. 2005). |
Our V5-Tag (SV5-Pk1) Antibody has been referenced in >215 publications* *Based on June 2020 data from CiteAb's antibody search engine. |
- Target Species
- Viral
- Product Form
- Purified IgG - liquid
- Preparation
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% sodium azide (NaN3)
- Carrier Free
- Yes
- Immunogen
- Paramyxovirus Simian-Virus 5 (SV5)
- Approx. Protein Concentrations
- IgG concentration 1 mg/ml
- Fusion Partners
- Spleen cells from immunised BALB/c mice were fused with cells of the SP2/0 Ag14 myeloma cell line.
- Regulatory
- For research purposes only
- Guarantee
- 12 months from date of despatch
- Acknowledgements
- This product is manufactued under an exclusive license from the University of St. Andrews, UK.
This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| ELISA |  |
1/1000 | 1/5000 |
| Flow Cytometry | |
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| Immunofluorescence | |
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| Immunohistology - Frozen | |
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| Immunoprecipitation | |
||
| Radioimmunoassays | |
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| Western Blotting | |
1/1000 | 1/5000 |
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
References for V5-Tag antibody
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Milward, A. et al. (2010) Hepatitis C virus NS5A protein interacts with beta-catenin and stimulates its transcriptional activity in a phosphoinositide-3 kinase-dependent fashion.
J Gen Virol. 91: 373-81.
View The Latest Product References
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- Synonyms
- PK-TAG
- RRID
- AB_322378
- UniProt
- P11207
- GO Terms
- GO:0003723 RNA binding
- GO:0046872 metal ion binding
- GO:0016070 RNA metabolic process
- GO:0030683 evasion by virus of host immune response
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