Anti c myc y69

Manufactured by Abcam

Sourced in United Kingdom

Anti-c-MYC-Y69 is an antibody that recognizes the c-MYC protein. The antibody is specific to the Y69 epitope of the c-MYC protein.

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Lab products found in correlation

Close spelling variants of this product

C-Myc (362 citations) Anti-c-Myc (157 citations) Anti-Myc (113 citations) C-Myc (Y69; (8 citations) MYC (Y69) (8 citations) Anti-MYC (Y69, (3 citations)

8 protocols using anti c myc y69

Western Blotting Antibody Panel

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Antibodies used for Western blotting were anti-FBW7α (#A301-720A), and anti-TRIP12 (#301-814A) from Bethyl laboratories (US), anti-vinculin (#V9131) from Sigma-Aldrich (St. Louis, MA, USA), anti-Actin HRP conjugated (#ab-49900), anti-GAPDH (#ab9485), anti-c-MYC-Y69 (#ab-32072) from Abcam (Cambridge, UK), anti-CyclinE (#sc-481) from Santa Cruz Biotechnology (Dallas, TX, USA), anti-MCL-1 (#54539) and anti-Cleaved caspase-7 (#9491) from Cell signaling technology (Denver, CO, USA).

Keyan K.S., Alanany R., Kohil A, & Khan O.M. (2023). E3 Ubiquitin Ligase TRIP12 Controls Exit from Mitosis via Positive Regulation of MCL-1 in Response to Taxol. Cancers, 15(2), 505.

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Western Blotting with Antibody Panel

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Western blotting was performed as previously described.²² The following antibodies were used: anti‐Alix (ABC40) from Millipore Sigma; anti‐Tsg101 (C‐2), anti‐CD63 (MX‐49.129.5), anti‐ATP6V1B1/2 (F‐6) and anti‐GAPDH (6C5) from Santa Cruz Biotechnology; anti‐phospho‐ERK1/2 (D13.14.4E), anti‐ERK1/2 (137F5), anti‐phospho‐MEK1/2 (41G9), anti‐MEK1/2 (L38C12), and anti‐Ras (27H5) from Cell Signaling Technology; anti‐c‐MYC (Y69) from Abcam; anti‐TFEB (PA5‐34360) from Thermo Fisher Scientific; and anti‐TFE3 (HPA023881) from Sigma‐Aldrich65. All antibodies were used at a 1:1000 dilution.

Hikita T., Uehara R., Itoh R.E., Mitani F., Miyata M., Yoshida T., Yamaguchi R, & Oneyama C. (2022). MEK/ERK‐mediated oncogenic signals promote secretion of extracellular vesicles by controlling lysosome function. Cancer Science, 113(4), 1264-1276.

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Immunoblotting Protein Detection Protocol

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Proteins from whole-cell lysates were detected by immunoblotting. Antibodies were from Cell Signaling Technology Inc. (Danvers, MA); p-AKT^Ser473 (#4060), p-4EBP1 (Thr37/46) (#2855), GAPDH (#2118), β-actin (#4970), p-NF-κB-p65 (#3033), p27^Kip1 (#3686), and p-IκBα (#2859). p-IKKα (S176/S180) was from R&D Systems (Minneapolis, MN). Rabbit-polyclonal-HBZ serum was previously reported,^{23 (link)} and Tax antibody was kindly gifted by Cynthia Masison (NCI/NIH). Anti-c-MYC [Y69] was from Abcam (Cambridge, MA). BATF3 (3H1) was from Novus Biologicals (Centennial, CO).

Daenthanasanmak A., Bamford R.N., Yoshioka M., Yang S.M., Homan P., Karim B., Bryant B.R., Petrus M.N., Thomas C.J., Green P.L., Miljkovic M.D., Conlon K.C, & Waldmann T.A. (2022). Triple combination of BET plus PI3K and NF-κB inhibitors exhibit synergistic activity in adult T-cell leukemia/lymphoma. Blood Advances, 6(7), 2346-2360.

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Western Blot Antibodies and Degron Constructs

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The following antibodies were used for western blotting: Anti-cMYC Y69 (Rabbit monoclonal Abcam ab32072), Anti-KRAS(G12V mutant specific D2H12) (Rabbit monclonal Cell Signaling Technologies (#14412), Anti-Phospho MEK-1 (T292) (Rabbit monoclonal Abcam ab76314),Anti-beta Actin (Mouse monoclonal abcam 8226, Mouse monoclonal Sigma Aldrich A1978), p21 (Rabbit monoclonal Cell Signaling Tech 12D1 2947S), EGFP (Rabbit polyclonal, Invitrogen A11122), Vinculin (Mouse monoclonal Sigma Aldrich, V9131), HA (Rabbit monoclonal Cell Signaling Technologies, 3724). IRDye® 680LT Goat anti-Mouse IgG (Licor, 926-68020) and IRDye® 800CW Goat anti-Rabbit IgG (Licor, 926-32211) were used as secondary antibodies.
The degron containing constructs were commercially synthetized (Invitrogen-GeneArt). Two back bones were used in this study: pLVX-puro for the doxycycline inducible systems and pHAGE-PGK DEST for the Flag-HA N terminally tagged constructs.

Bouguenina H., Nicolaou S., Le Bihan Y.V., Bowling E.A., Calderon C., Caldwell J.J., Harrington B., Hayes A., McAndrew P.C., Mitsopoulos C., Sialana F.J., Scarpino A., Stubbs M., Thapaliya A., Tyagi S., Wang H.Z., Wood F., Burke R., Raynaud F., Choudhary J., van Montfort R.L., Sadok A., Westbrook T.F., Collins I, & Chopra R. (2023). iTAG an optimized IMiD-induced degron for targeted protein degradation in human and murine cells. iScience, 26(7), 107059.

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Western Blotting Antibody Panel

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Antibodies used for western blotting were anti-FBW7α (#A301-720A), and anti-TRIP12, 1:500 (#301-814A) from Bethyl, anti-FLAG, 1:5000 (#M2 clone), anti-HA-HRP-conjugate, 1:5000 (#A190108P), anti-c-MYC Tag, 1:500 (#clone4A6) HRP conjugated, and anti-vinculin, 1:1000 (#V9131) from Sigma, anti-GFP, 1:1000 (#11814460001, Roche), anti-Actin HRP-conjugate, 1:10,000 (#ab-49900), anti-GAPDH, 1;1000 (#ab9485), anti-c-MYC-Y69, 1:1000 (#ab-32072), and anti-α-tubulin, 1:2000 (#ab-7291) from Abcam, anti-CUL1, 1:1000 (#71-8700, Invitrogen), anti-p19Skp1, 1:1000 (#610530, BD Biosciences), anti-CyclinE, 1:1000 (#sc-481), and anti-RNF168, 1:1000 (#sc-101125) from Santa Cruz, anti-CDKN2a, 1:1000 (#4824), phospho-p42/44 MAPK, 1:1000 (#4376), and anti-MCL1, 1:1000 (#54539) from Cell signaling, anti-conjugated ubiquitin (FK2, 1:1000) (#BML-PW8810, Enzo life sciences), and anti-Lys11 linkage-specific, 1:500 (#MABS107), was from Millipore.

Khan O.M., Almagro J., Nelson J.K., Horswell S., Encheva V., Keyan K.S., Clurman B.E., Snijders A.P, & Behrens A. (2021). Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12. Nature Communications, 12, 2043.

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Immunohistochemical Profiling of Lymphoma

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Paraffin‐embedded sections of each sample were subjected to IHC staining, using anti‐CD10 (56C6; Leica Microsystems), anti‐CD20 (L‐26; DakoCytomation), anti‐B‐cell lymphoma 2 (BCL2) (124; DakoCytomation), anti‐BCL6 (P1F6; Leica Microsystems), anti‐MUM1 (MUM1p; DakoCytomation), and anti‐c‐MYC (Y69; Abcam) Abs. Each case was considered as positive if more than approximately 30% neoplastic cells were positive, except for BCL2 and MYC, for which each case was considered positive if more than approximately 50% and 40% neoplastic cells were positive, respectively.¹⁷ Tumors coexpressing the MYC and BCL2 proteins were considered as double expressor lymphomas (DELs).¹⁷ Immunohistochemical staining was also undertaken with the anti‐CD68 Ab (KP‐1; DakoCytomation) as the panmacrophage marker and the anti‐CD163 Ab (10D6; Leica Microsystems) for the M2 macrophage. The number of CD68‐ and CD163‐positive cells was evaluated in a representative high‐power field corresponding to that of SIRPα.

Kazama R., Miyoshi H., Takeuchi M., Miyawaki K., Nakashima K., Yoshida N., Kawamoto K., Yanagida E., Yamada K., Umeno T., Suzuki T., Kato K., Takizawa J., Seto M., Akashi K, & Ohshima K. (2020). Combination of CD47 and signal‐regulatory protein‐α constituting the “don’t eat me signal” is a prognostic factor in diffuse large B‐cell lymphoma. Cancer Science, 111(7), 2608-2619.

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Immunohistochemical Profiling of DLBCL

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Tissue samples were processed as formalin‐fixed, paraffin‐embedded tissues according to standard institutional procedures. We created tissue microarrays from samples from 61 patients and undertook evaluations of IHC with antibodies using these microarrays. Antibodies (clones) used for IHC included anti‐CD20 (L‐26; DakoCytomation, Glostrup, Denmark), anti‐BCL2 (clone124; DakoCytomation), anti‐BCL6 (P1F6; Leica Microsystems, Wetzlar, Germany), anti‐Multiple myeloma oncogene ‐1 (MUM ‐1) (MUM1p; DakoCytomation), anti‐CD10 (56C6; Leica Microsystems), and anti‐c‐MYC (Y69) antibodies (Abcam, Cambridge, UK). Immunohistochemistry results were reviewed by two expert hematopathologists (H.M. and K.O.). Cut‐off points for MYC, BCL2, and BCL6 protein expression were defined as DLBCL with 30% or more, 1% or more, and 30% or more positive cells, respectively, as recommended in previous studies.12, 15, 34

Kawamoto K., Miyoshi H., Yoshida N., Nakamura N., Ohshima K., Sone H, & Takizawa J. (2016). MYC translocation and/or BCL 2 protein expression are associated with poor prognosis in diffuse large B‐cell lymphoma. Cancer Science, 107(6), 853-861.

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Mitochondrial and Cell Protein Profiling

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5 to 10×10⁶ cells were lysed with RIPA buffer (50mM Tris-cl pH7.6, 1%NP40, 1% deoxycholic acid, 0.1% SDS, 1mM EDTA, 150mM NaCl) supplemented with protease and phosphatase inhibitors (Roche), sonicated in a water bath sonicator and cleared by centrifugation at 13000xg. 30 μg of cleared lysates were electrophoresed on SDS-PAGE gels and immunoblotted with the following primary antibodies: mouse monoclonal anti-Complex I subunit NDUFB8 (Invitrogen, cat. #459210); mouse monoclonal anti-Complex III subunit UQCRC2 (Abcam, cat. #ab14745); rabbit polyclonal anti-VDAC (Pierce, cat. #PA1-954A); mouse monoclonal anti-MT-COI (MitoScience, cat. #1D6E1A8); mouse monoclonal anti-SDHA (Invitrogen, cat. #459200); mouse monoclonal anti COX IV (Abcam, cat. #ab33985); rabbit monoclonal anti-c-Myc Y69 (Abcam, cat. #GR144732-28); mouse monoclonal anti-vinculin (Abcam, cat. #ab18058). After incubation of the membranes with appropriate secondary antibodies, chemiluminescent detection was done through a CCD camera using the ChemiDoc System (Bio-Rad). Quantification of protein levels was done using the Image Lab software.

D'Andrea A., Gritti I., Nicoli P., Giorgio M., Doni M., Conti A., Bianchi V., Casoli L., Sabò A., Mironov A., Beznoussenko G.V, & Amati B. (2016). The mitochondrial translation machinery as a therapeutic target in Myc-driven lymphomas. Oncotarget, 7(45), 72415-72430.

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