Anti acetyl lysine

Manufactured by Merck Group

Anti-Acetyl-lysine is a lab equipment product that functions as an antibody. It is used to detect and quantify acetylated lysine residues in proteins.

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Lab products found in correlation

Mouse monoclonal anti acetylated α tubulin clone 6 11b 1, by Merck Group (2 mentions) Ecl prime kit, by GE Healthcare (1 mentions) Ecl reagent, by Merck Group (1 mentions) Anti lc3b, by Proteintech (1 mentions) Anti sirt1, by Merck Group (1 mentions) Anti α synuclein, by Abcam (1 mentions) Protein a agarose beads, by Beyotime (1 mentions) Anti tyrosine hydroxylase, by Merck Group (1 mentions) Anti p62, by Proteintech (1 mentions) Anti gapdh, by Proteintech (1 mentions) Trans blot cell, by Bio-Rad (1 mentions) Immobilion pvdf membranes, by Merck Group (1 mentions) Memcode, by Thermo Fisher Scientific (1 mentions) Collagen 1 and collagen 3, by Abcam (1 mentions) Serca2a, by Thermo Fisher Scientific (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Cox 2, by Cayman Chemical (1 mentions) Human sirt1, by Santa Cruz Biotechnology (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Santa Cruz Biotechnology (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions)

7 protocols using anti acetyl lysine

Western Blot Analysis of T. cruzi Proteins

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Protein extracts were fractioned in SDS-PAGE and transferred to nitrocellulose membranes. Transferred proteins were visualized with Ponceau S. Membranes were treated with 10% non-fat milk in PBS for 2 hours and then incubated with specific antibodies diluted in PBS for 3 hours. Antibodies used were: rat monoclonal anti-HA (ROCHE), rabbit polyclonal anti-TcSIR2RP1 and anti-TcSIR2RP3, rabbit polyclonal anti-Acetyl-lysine (Millipore), mouse monoclonal anti-acetylated α-tubulin clone 6-11B-1 (Sigma Aldrich), mouse monoclonal anti-trypanosome α-tubulin clone TAT-1, rabbit polyclonal anti-T. cruzi mitochondrial Malate Dehydrogenase (TcMDHm), rabbit and mouse polyclonal anti-T. cruzi Tyrosine Amine Transferase (TcTAT), mouse polyclonal anti-T. cruzi Aspartate Transaminase (TcASAT) and rabbit polyclonal anti-T. cruzi Bromodomain Factor 2 (TcBDF2). Bound antibodies were detected using peroxidase labeled anti-mouse, anti-rabbit IgGs (GE Healthcare) or anti-rat IgG (Thermo Scientific) and developed using ECL Prime kit (GE Healthcare) according to manufactures protocol.

Ritagliati C., Alonso V.L., Manarin R., Cribb P, & Serra E.C. (2015). Overexpression of Cytoplasmic TcSIR2RP1 and Mitochondrial TcSIR2RP3 Impacts on Trypanosoma cruzi Growth and Cell Invasion. PLoS Neglected Tropical Diseases, 9(4), e0003725.

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Western blot and immunoprecipitation of brain proteins

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Dissected mouse brain tissues were lysed in RIPA buffer and the protein homogenates were then separated by SDS-PAGE and transferred onto a polyvinylidene fluoride membrane. After blocking, the membranes were incubated overnight with primary antibodies, followed by washing and incubation with horseradish peroxidase conjugated secondary antibody for 1 h. Immunoreactive bands were then visualized using the ECL reagent (WBKLS0100, Merck Millipore). The densities of the immunoblotting bands were semiquantified using Image J software (National Institutes of Health). The primary antibodies used were as follows: anti-tyrosine hydroxylase (TH) (#T2928, Sigma), anti-α-synuclein (#ab1903, Abcam), anti-SIRT1 (#07–131, Millipore), anti-p62 (#18420–1-AP, Protein Tech Group), anti-LC3B (#18725–1-AP, Protein Tech Group), anti-acetyl-Lysine (#05–515, Millipore), anti-caspase-3 (#9662, CST), and anti-GAPDH (#10494–1-AP, Protein Tech Group).
For immunoprecipitation, extracted proteins were incubated with anti-LC3B (#3868, CST) at 4°C overnight with rotation, followed by precipitation with protein A agarose beads (P2012, Beyotime). Immunoprecipitates were then washed and subjected to SDS-PAGE separation. Subsequent immunoblotting procedures were the same as described above.

Guo Y.J., Dong S.Y., Cui X.X., Feng Y., Liu T., Yin M., Kuo S.H., Tan E.K., Zhao W.J, & Wu Y.C. (2016). Resveratrol alleviates MPTP-induced motor impairments and pathological changes by autophagic degradation of α-synuclein via SIRT1-deacetylated LC3. Molecular nutrition & food research, 60(10), 2161-2175.

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Western Blot Analysis of Cardiac Proteins

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Western analysis was performed on flash frozen LV samples as previously described44 (link)45 (link) using the following primary antibodies: SERCA2a (Thermo Scientific), NCX1 (Thermo scientific), collagen-I and collagen-III (Abcam), sirtuin-1 and FOXO1 (Cell signaling Inc), total and phospho (threonine-172) AMPK (Cell signaling Inc), and subsequently incubated with HRP conjugated secondary antibodies31 (link). Immunoprecipitation was performed with slight modification as described previously31 (link). Total protein lysate (100–200 μg) from flash frozen LV were incubated with 5 μg of anti-acetyl-Lysine (Millipore). The immune complex was captured by adding 50 μl protein A/G Plus-agarose beads (Sc-2003) with gentle rocking for 6 hr at 4 °C; the tubes were then centrifuged at 12000 g for 3 min and the supernatants were discarded. The pellets were gently washed with ice cold PBS and the immune complex resuspended in 60 μl of 2X Laemmli sample buffer and resolved on 8% SDS-PAGE then transferred to Immobilion PVDF membranes (Millipore) using a Trans-blot cell (Bio-Rad laboratories, Hercules CA, USA). Membranes were stained for total amount of protein as a loading control using MemCode (Thermo Scientific).

Das S.K., Wang W., Zhabyeyev P., Basu R., McLean B., Fan D., Parajuli N., DesAulniers J., Patel V.B., Hajjar R.J., Dyck J.R., Kassiri Z, & Oudit G.Y. (2015). Iron-overload injury and cardiomyopathy in acquired and genetic models is attenuated by resveratrol therapy. Scientific Reports, 5, 18132.

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Western Blot Analysis of Cellular Proteins

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Cellular protein was extracted with RIPA buffer (25 mM Tris-HCl pH 7.6, 150 mM NaCl, 1% NP-40, 1% sodium deoxycholate, 0.1% SDS). After complete homogenization on ice, samples were sonicated and centrifuged at 4°C. The supernatants were transferred into fresh tubes and protein concentrations were detected by the BCA method. Equal amounts of protein (20 µg/lane) were separated by SDS-PAGE and transferred onto polyvinylidenedifluoride membranes (Millipore). After blocking with 5% non-fat milk, the filters were incubated overnight at 4°C with the primary antibodies against HA (Sigma-Aldrich), β-actin (Sigma-Aldrich), GAPDH (Cell Signaling Technology), Myc (Santa Cruz), human SIRT1 (Santa Cruz), Anti-acetyl-lysine (Millipore) and COX-2 (Cayman Chemicals). After washing and incubating with the appropriate horseradish-peroxidase-conjugated secondary antibody (Santa Cruz), the immune complexes were visualized with a chemiluminescent reagent. Western blots were quantified by the intensity values and were normalized to GAPDH or β-actin.

Jia Y.Y., Lu J., Huang Y., Liu G., Gao P., Wan Y.Z., Zhang R., Zhang Z.Q., Yang R.F., Tang X., Xu J., Wang X., Chen H.Z, & Liu D.P. (2014). The Involvement of NFAT Transcriptional Activity Suppression in SIRT1-Mediated Inhibition of COX-2 Expression Induced by PMA/Ionomycin. PLoS ONE, 9(5), e97999.

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Western Blot and Immunoprecipitation Protocol

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Western blotting was performed as described [36 (link)]. The following primary antibodies were used: HDAC10 (H3413, Sigma), P27 (N-20) (sc-527, Santa Cruz), P21 (ab7960, Abcam), Cyclin D1 (sc-718, Santa Cruz), Cyclin E1 (sc-481, Santa Cruz), AKT (#4685S, CST), p-AKT (#4060S, CST), BCL-2 (21060, SAB), BAK (BS1029, Bioworld), Anti-HA (AP0005, Bioworld), GAPDH (sc-47724, Santa Cruz), and Anti-Acetyl-lysine (Millipore, 06-933). The following secondary antibodies were used: HRP-Ms (#7074, CST) and HRP-Rb (#7076, CST). For immunoprecipitation (IP), Anti-HA beads (E6779, Sigma), Anti-M2 beads (F2426, Sigma), normal IgG (#2729, CST), and protein A/G beads (16-125, Millipore) were used. IP was performed as described in [36 (link)]. Briefly, the cells were harvested and lysed in lysis buffer (50 mM Tris, pH 7.4, 120 mM NaCl, 0.5 mM EDTA, 0.5% Nonidet P-40, and 15% glycerol) supplemented with protease inhibitors (1 mM phenylmethylsulfonyl fluoride, 0.7 μg/ml pepstatin A, 2 μg/ml aprotinin, 2 mM NaF, and 1 mM Na3VO4). Endogenous AKT or HDAC10 was IPed with antibodies and protein A/G beads. For immunofluorescence staining, the cells were seeded on glass coverslips (12-545-82, Thermo Fisher) and stained as described in [36 (link)].

Yang Y., Huang Y., Wang Z., Wang H.T., Duan B., Ye D., Wang C., Jing R., Leng Y., Xi J., Chen W., Wang G., Jia W., Zhu S, & Kang J. (2016). HDAC10 promotes lung cancer proliferation via AKT phosphorylation. Oncotarget, 7(37), 59388-59401.

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Protein Expression and Immunoblotting Analysis

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Protein extracts were fractioned in SDS-PAGE and transferred to a nitrocellulose membrane. Transferred proteins were visualized with Ponceau S staining. Membranes were treated with 10% non-fat milk in PBS for 2 h and then incubated with specific antibodies diluted in 0.5% Tween 20 in PBS (PBS-T) for 3 h. Primary antibodies used were: rat monoclonal anti-HA 1:2000 (ROCHE), affinity-purified rabbit polyclonal anti-TcATAT 1:200, mouse monoclonal anti-trypanosome α-tubulin clone TAT-1 1:1000 (a gift from K. Gull, University of Oxford, UK), rabbit polyclonal anti-Acetyl-lysine 1:1000 (Millipore), mouse monoclonal anti-acetylated α-tubulin clone 6-11B-1 1:2000 (Sigma Aldrich). Bound antibodies were detected using peroxidase-labeled anti-rabbit IgG (GE Healthcare), anti-mouse IgG (GE Healthcare) or anti-rat IgG (Thermo Scientific) and developed using ECL Plus kit (GE Healthcare) according to manufacturer’s protocols. Immunoreactive bands were visualized and photographed in the Amersham Imager 600 (GE Healthcare). Images were processed and bands where quantified with ImageJ (Schindelin et al., 2012 (link)).

Alonso V.L., Carloni M.E., Gonçalves C.S., Martinez Peralta G., Chesta M.E., Pezza A., Tavernelli L.E., Motta M.C, & Serra E. (2021). Alpha-Tubulin Acetylation in Trypanosoma cruzi: A Dynamic Instability of Microtubules Is Required for Replication and Cell Cycle Progression. Frontiers in Cellular and Infection Microbiology, 11, 642271.

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Epigenetic Regulatory Protein Analysis

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Antibodies obtained from Cell Signaling Technology (Danvers, MA) included HDAC1 (5356), HDAC2 (2545), and HDAC3 (2632). β‐Actin (A‐2228) was obtained from Sigma‐Aldrich The antibody SUZ12 (catalog number: sc‐46264) was purchased from Santa Cruz Biotechnology (Santa Cruz, CA). Anti‐EED (catalog number: 09‐774) and anti‐acetyl‐lysine (catalog number: 05‐515) were purchased from Millipore (Temecula, CA). The c‐Myc antibody (catalog number: 11667149001) was purchased from Roche Molecular Biochemicals (Indianapolis, IN).

Shi B., Behrens C., Vaghani V., Riquelme E.M., Rodriguez‐Canales J., Kadara H., Lin H., Lee J., Liu H., Wistuba I, & Simon G. (2019). Oncogenic enhancer of zeste homolog 2 is an actionable target in patients with non‐small cell lung cancer. Cancer Medicine, 8(14), 6383-6392.

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