For immunochemical detection of acetyl lysine
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Acetyl Lysine Monoclonal Antibody (Clone RM101)

Item No. 32125

Technical Information
Synonyms
  • ACE
Immunogen
Acetyl lysine-BSA
Clone Designation
RM101
100 µg of protein A-affinity purified monoclonal antibody
Storage Buffer
PBS with 50% glycerol, 1% BSA, and 0.09% sodium azide
Host
Rabbit
Isotype
IgG
Applications
ChIP, ICC, IHC, IP, WB
Cross Reactivity
(+) Lysine-acetylated proteins(-) Non-acetylated lysine residues(-) Lysine residues with other modifications
Species Reactivity
(Independent) Species
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Lysine acetylation is an evolutionarily conserved post-translational modification that is found in prokaryotes and eukaryotes at histone and non-histone protein sites.1 Transfer of an acetyl group from acetyl-coenzyme A (acetyl-CoA) to the amino side chain of lysine is catalyzed by lysine acetyltransferases (KATs), including 13 canonical KATs from the GCN5, p300, and MYST families. Acetyl lysine removal is catalyzed by two major groups of lysine deacetylases (KDACs), the zinc-dependent histone deacetylases (HDACs) and the NAD+-dependent sirtuin deacetylases. Histone acetylation is associated with active gene transcription, and dysregulation of histone acetylation is associated with various diseases including cancer, Huntington's and Alzheimer's diseases, and amyotrophic lateral sclerosis (ALS).2,3,4 Non-histone protein acetylation is linked to various cellular processes including autophagy, DNA replication, lipid storage, mitochondrial fission and fusion, and protein synthesis, among others.1 Cayman’s Acetyl Lysine Monoclonal Antibody (Clone RM101) can be used for immunocytochemistry (ICC), immunohistochemistry (IHC), immunoprecipitation (IP), chromatin immunoprecipitation (ChIP), and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Narita, T., Weinert, B.T., and Choudhary, C. Functions and mechanisms of non-histone protein acetylation. Nat. Rev. Mol. Cell Biol. 20(3), 156-174 (2019).

    2. Audia, J.E., and Campbell, R.M. Histone modifications and cancer. Cold Spring Harb. Perspect. 8(4), a019521 (2016).

    3. Bonnaud, E.M., Suberbielle, E., and Malnou, C.E. Histone acetylation in neuronal (dys)function. Biomol. Concepts 7(2), 103-116 (2016).

    4. Bennett, S.A., Tanaz, R., Cobos, S.N., et alEpigenetics in amyotrophic lateral sclerosis: A role for histone post-translational modifications in neurodegenerative disease. Transl. Res. 204, 19-30 (2019).