Antibody data
- Antibody Data
- Antigen structure
- References [7]
- Comments [0]
- Validations
- Western blot [2]
- Flow cytometry [1]
- Other assay [3]
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Validation data
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- Product number
- AHO0052 - Provider product page
- Provider
- Invitrogen Antibodies
- Product name
- c-Myc Monoclonal Antibody (9 E11)
- Antibody type
- Monoclonal
- Antigen
- Synthetic peptide
- Reactivity
- Human, Mouse, Chicken/Avian
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- 9 E11
- Vial size
- 100 µg
- Concentration
- 0.2 mg/mL
- Storage
- 4° C
Submitted references Specific Deubiquitinating Enzymes Promote Host Restriction Factors Against HIV/SIV Viruses.
Anti- c-myc cholesterol based lipoplexes as onco-nanotherapeutic agents in vitro.
Human cytomegalovirus UL141 protein interacts with CELF5 and affects viral DNA replication.
LRIG1 opposes epithelial-to-mesenchymal transition and inhibits invasion of basal-like breast cancer cells.
Auxin-inducible protein depletion system in fission yeast.
Novel functional residues in the core domain of histone H2B regulate yeast gene expression and silencing and affect the response to DNA damage.
Genetic and genomewide analysis of simultaneous mutations in acetylated and methylated lysine residues in histone H3 in Saccharomyces cerevisiae.
Gao W, Rui Y, Li G, Zhai C, Su J, Liu H, Zheng W, Zheng B, Zhang W, Yang Y, Hua S, Yu X
Frontiers in immunology 2021;12:740713
Frontiers in immunology 2021;12:740713
Anti- c-myc cholesterol based lipoplexes as onco-nanotherapeutic agents in vitro.
Habib S, Daniels A, Ariatti M, Singh M
F1000Research 2020;9:770
F1000Research 2020;9:770
Human cytomegalovirus UL141 protein interacts with CELF5 and affects viral DNA replication.
Zou F, Lu ZT, Wang S, Wu S, Wu YY, Sun ZR
Molecular medicine reports 2018 Mar;17(3):4657-4664
Molecular medicine reports 2018 Mar;17(3):4657-4664
LRIG1 opposes epithelial-to-mesenchymal transition and inhibits invasion of basal-like breast cancer cells.
Yokdang N, Hatakeyama J, Wald JH, Simion C, Tellez JD, Chang DZ, Swamynathan MM, Chen M, Murphy WJ, Carraway Iii KL, Sweeney C
Oncogene 2016 Jun 2;35(22):2932-47
Oncogene 2016 Jun 2;35(22):2932-47
Auxin-inducible protein depletion system in fission yeast.
Kanke M, Nishimura K, Kanemaki M, Kakimoto T, Takahashi TS, Nakagawa T, Masukata H
BMC cell biology 2011 Feb 11;12:8
BMC cell biology 2011 Feb 11;12:8
Novel functional residues in the core domain of histone H2B regulate yeast gene expression and silencing and affect the response to DNA damage.
Kyriss MN, Jin Y, Gallegos IJ, Sanford JA, Wyrick JJ
Molecular and cellular biology 2010 Jul;30(14):3503-18
Molecular and cellular biology 2010 Jul;30(14):3503-18
Genetic and genomewide analysis of simultaneous mutations in acetylated and methylated lysine residues in histone H3 in Saccharomyces cerevisiae.
Jin Y, Rodriguez AM, Wyrick JJ
Genetics 2009 Feb;181(2):461-72
Genetics 2009 Feb;181(2):461-72
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Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Western blot was performed using Anti-Myc Tag Monoclonal Antibody (Product # AHO0052) by loading whole cell extracts of untransfected and transiently transfected HEK-293E lysates: untransfected, 60 µg (Lane 1), empty vector control, 60 µg (Lane 2), Myc-p65-V5, 60 µg (Lane 3), Myc-p65-V5, 40 µg (Lane 4), Myc-p65-V5, 20 µg (Lane 5), p65-HA, 60 µg (Lane 6) and 25 ng of Positope (Lane 7) were electrophoresed using NuPAGE™ 4-12% Bis-Tris Protein Gel (Product # NP0321BOX). Resolved proteins were then transferred onto a nitrocellulose membrane (Product # IB23001) by iBlot® 2 Dry Blotting System (Product # IB21001). A ~65 kDa band corresponding to Myc-p65-V5 was observed in HEK293E transfected lysates on probing with the primary antibody (1:1000 dilution) and detected by chemiluminescence with Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, HRP (Product # A28177, 1:4000 dilution) . Positope (Product # R90050). Positope (Product # R90050) is a 53 kDa recombinant protein consisting multiple epitope tags, which has been used as a positive control for Myc detection. No cross-reactivity was seen with p65-HA expressing lysate.
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Western Blot was performed using Anti-Myc Tag Monoclonal Antibody (Product # AHO0052) by loading whole cell extracts of untransfected and transiently transfected HEK-293E lysates: untransfected, 60 µg (Lane 1), empty vector control, 60 µg (Lane 2), Myc-p65-V5, 60 µg (Lane 3), Myc-p65-V5, 40 µg (Lane 4), Myc-p65-V5, 20 µg (Lane 5), FLAG-p65-HA, 60 µg (Lane 6) and 25 ng of Positope (Lane 7) were electrophoresed using NuPAGE™ 4-12% Bis-Tris Protein Gel (Product # NP0321BOX). Resolved proteins were then transferred onto a nitrocellulose membrane (Product # IB23001) by iBlot® 2 Dry Blotting System (Product # IB21001). A ~65 kDa band corresponding to Myc-p65-V5 was observed in HEK293E transfected lysates on probing with the primary antibody (1:1000 dilution) and detected by chemiluminescence with Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, HRP (Product # A28177, 1:4000 dilution) . Chemiluminescent detection was performed using Novex® ECL Chemiluminescent Substrate Reagent Kit (Product # WP20005). Positope (Product # R90050). Positope (Product # R90050) is a 53 kDa recombinant protein consisting multiple epitope tags, which has been used as a positive control for Myc detection. No cross-reactivity was seen with FLAG-HA-tagged p65 expressing lysate.
Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Flow cytometry analysis of c-Myc was done on Jurkat cells. Cells were fixed with 70% ethanol for 10 minutes, permeabilized with 0.25% Triton™ X-100 for 20 minutes, and blocked with 5% BSA for 30 minutes at room temperature. Cells were labeled with c-Myc Mouse Monoclonal Antibody (AHO0052, red histogram) or with mouse isotype control (pink histogram) at 3-5 ug/million cells in 2.5% BSA. After incubation at room temperature for 2 hours, the cells were labeled with Alexa Fluor® 488 Rabbit Anti-Mouse Secondary Antibody (A11059) at a dilution of 1:400 for 30 minutes at room temperature. The representative 10,000 cells were acquired and analyzed for each sample using an Attune® Acoustic Focusing Cytometer. The purple histogram represents unstained control cells and the green histogram represents no-primary-antibody control.
Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- NULL
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Figure 8. Effect of anti- c-myc lipoplexes on c-myc protein expression in a) MCF-7 and b) HT-29 cells, following transfection with MS09:DOPE and MS09:Chol lipoplexes. c-myc expression was quantified by ELISA, and normalized to the internal control, beta-actin. Each column represents the mean +- SD ( n = 3). * P < 0.05, *** P < 0.001 vs . naked siRNA; P < 0.05, P < 0.001 vs . non-targeting siRNA; # P 0.05, with respect to anti c-myc MS09:Chol vs . anti- c-myc MS09:DOPE. LF3K= Lipofectamine (tm) 3000.
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Figure 3 Ubiquitin-specific protease 8 (USP8) specifically interacts with HIV-1 virion infectivity factor (Vif) and reduces Vif-triggered apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3)G (A3G) polyubiquitination. (A) Co-precipitation of USP8 with Vif. HEK293T cells were transfected with USP8-HA, Vif-Myc alone, or both, as indicated. Cell lysates were prepared and immunoprecipitated using anti-Myc antibody conjugated to agarose beads 48 h after transfection. Cell lysates and precipitated samples were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to nitrocellulose membranes, and reacted with an anti-HA antibody to detect USP8-HA and an anti-Myc antibody to detect Vif-Myc. Tubulin was used as the loading control for the cell lysate. (B) USP8 does not affect Vif-CRL5 E3 ubiquitin ligase formation. HEK293T cells were transfected with Vif-Myc, USP8-HA, or both. Cell lysates were immunoprecipitated with anti-Myc antibodies conjugated to agarose beads. Cell lysates and precipitated samples were analyzed by immunoblotting with the corresponding antibodies. Tubulin was used as the loading control for the cell lysate. (C) Relative binding ability of Vif with Cul5, CBFbeta, and EloB in the presence or absence of USP8 was determined by ImageJ2X. Protein binding to Vif in lane 2 (B , upper blots ) was set to 1.0. Data are means +- SD from n = 3 independent experiments. The statistical significance analyses were pe