Acetyl Lysine Antibody Mouse Monoclonal

Acetyl Lysine Mouse Monoclonal Antibody
$0.00

Host/Isotype
Mouse / IgG2b

Clone
3C6.08.20

Species Reactivity
All species

RRID 

AB_2884959

Anti-acetyl lysine antibody is a pan-acetyl lysine mouse monoclonal antibody that is part of the Signal-Seeker™ product line.The Anti-acetyl-lysine antibody recognizes proteins post-translationally modified by acetylation on the epsilon amine groups of lysine residues that occur on 30-50% of all proteins and in particular histones, p53, tubulin and myosin. A proprietary mixture of acetylated proteins was used to produce a highly robust antibody that has been shown to recognize a wide range of acetylated proteins in IP, WB, ChIP and IF applications. This Anti-acetyl-lysine antibody has many advantages when compared to other commercially available antibodies as shown below.


Validated Applications

Western Blot using Acetyl Lysine Antibody

Cytoskeleton's Anti-Acetyl Lysine Antibody Cat. # AAC01 recognizes 0.005 ng of chemically acetylated BSA and is comparable in sensitivity to other commercially available antibodies.  Unlike other Anti-Acetyle Lysine antibodies this antibody does not show cross reactivity with non-acetylated BSA.  To see the full Western blot comparison, see the Optimized Protocols or the product datasheet.

Acetyl Lysine Western Blot

Immunoprecipitation using Acetyl Lysine Antibody

Ability of AAC01 to IP histones was compared to other commercially available antibodies.  Cytoskeleton's Anti-Acetyl Lysine Antibody provides clear advantages for IP applications. Each tube is sufficient for approximately 20 IP assays.  To see the full Immunoprecipitation comparison, see the Optimized Protocols or the product datasheet.

Acetyl Lysine Immunoprecipitation
Immunofluorescence using Acetyl Lysine Antibody
 
Human epidermoid carcinoma A431 cells, untreated (top) or treated (bottom) with TSA (5 mM for 12 h), were stained as described in the method. Acetylated cytoplasmic and nuclear proteins were visualized in green fluorescence. Note that in contrast with the untreated control, acetylated microtubule network is clearly visible in TSA-treated sample. The fluorescent nuclear  intensities indicate the high abundance of acetylated proteins in the nucleus. To see the full Immunofluorescence protocol, see the Optimized Protocols or the product datasheet.
Acetyl Lysine IF
ChIP using Acetyl Lysine Antibody

Chromatin was prepared from A431 cells, either untreated or TSA-treated (5 mM, 4 hrs). Briefly, cells were fixed with 1% formaldehyde for 10 min and enzymatically-sheared chromatins were immunoprecipitated by using anti-acetyl antibodies (1:100 dilution). The promoter region of housekeeping gene GAPDH was amplified by a primer pair and PCR products were analyzed by 2% agarose gel-electrophoresis.  To see the recommended ChIP protocol, see the Optimized Protocols or the product datasheet.

Acetyl Lysine ChIP

Protein Acetylation Background

Acetylation of proteins can occur as a co-translational or post-translational modification  (PTM) (1).  Co-translational acetylation occurs at the N-terminal of approximately 85% of mammalian proteins, it is irreversible and is thought to be important in protein stability, localization and synthesis (1).  Post-translational acetylation occurs on the epsilon amino group of lysine residues as a reversible and highly dynamic PTM that is known to be a key regulator in multiple cellular events, including chromatin structure, transcription,  metabolism,  signal transduction and cytoskeletal regulation (2-3).  To date over 4,000 proteins have been identified as targets for PTM acetylation which is comparable to phosphorylation in cellular prevelance (3).  Antibody AAC01 detects acetyl lysine PTMs. 

 

References

1 Bogdan P. and Sherman F. 2002. The diversity of acetylated proteins. Genome Biol. 3 (5): reviews 0006.

2 Lundby A. et al. 2012. Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and cellular patterns. Cell Reports 2:419-431.

3 Sadoul K. et al. 2010. The tale of protein lysine acetylation in the cytoplasm.  J. Biomed. Biotech. 2011:1-15.

4 Golemis EA et. Al, Protein-Protein Interactions, CSHLP, 2005, p67

For more information contact:  signalseeker@cytoskeleton.com

Associated Products:

Signal-Seeker™: BlastR™ Rapid Lysate Prep Kit (Cat. # BLR01)

For product Datasheets, MSDSs, and COAs please click on the PDF links below.

 

Sample Size Datasheet (Cat. AAC01-S):  

Certificate of Analysis:  Lot 013

 

AuthorTitleJournalYearArticle Link
Martins, Vitor F. et al.p300 or CBP is required for insulinstimulated glucose uptake in skeletal muscle and adipocytesJCI Insight2022ISSN 2379-3708
Martins, Vitor F. et al.Germline or inducible knockout of p300 or cbp in skeletal muscle does not alter insulin sensitivityAmerican Journal of Physiology - Endocrinology and Metabolism2019ISSN 1522-1555
Sharma, Monica et al.Acetylation of conserved DVL-1 lysines regulates its nuclear translocation and binding to gene promoters in triple-negative breast cancerScientific Reports2019ISSN 2045-2322
Ishihara, Akinori et al.Seasonal acclimatization and thermal acclimation induce global histone epigenetic changes in liver of bullfrog (Lithobates catesbeianus) tadpoleComparative Biochemistry and Physiology -Part A : Molecular and Integrative Physiology2019ISSN 1531-4332
Yang, Youyun et al.Identification of acetylated proteins in Borrelia burgdorferiMethods in Molecular Biology2018ISSN 1064-3745
Horita, Henrick et al.Utilizing a comprehensive immunoprecipitation enrichment system to identify an endogenous post-translational modification profile for target proteinsJournal of Visualized Experiments2018ISSN 1940-087X
Horita, Henrick et al.A simple toolset to identify endogenous post-translational modifications for a target protein: A snapshot of the EGFR signaling pathwayBioscience Reports2017ISSN 1573-4935
Horita, Henrick et al.Identifying Regulatory Posttranslational Modifications of PD-L1: A Focus on MonoubiquitinatonNeoplasia (United States)2017ISSN 1476-5586
LaBarge, Samuel A. et al.P300 is not required for metabolic adaptation to endurance exercise trainingFASEB Journal2016ISSN 1530-6860

Visit our Signal-Seeker™ Tech Tips and FAQs page for technical tips and frequently asked questions regarding this and other Signal-Seeker™ products click here

 

If you have any questions concerning this product, please contact our Technical Service department at tservice@cytoskeleton.com