For immunochemical detection of acetyl lysine
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Acetyl Lysine Monoclonal Antibody (Clone 7F8)

Item No. 10010567

Technical Information
Synonyms
  • ACE
Immunogen
Acetylated KLH
Clone Designation
7F8
100 µg of ammonium sulfate precipitated monoclonal antibody
Storage Buffer
TBS, pH 7.4, with 50% glycerol, 0.1% BSA, and 0.02% sodium azide
Host
Mouse
Isotype
IgG1
Applications
ELISA, ICC, WB
Cross Reactivity
(-) Non-acetylated lysine residues
Origin
Animal/Mouse
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 posttranslational 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 7F8) can be used for ELISA, immunocytochemistry (ICC), and Western blot 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).