A peptide fragment of histone H3
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Histone H3K79Ac (73-83) (human, mouse, rat, porcine, bovine) (trifluoroacetate salt)

Item No. 27489

Technical Information
Formal Name
L-α-glutamyl-L-isoleucyl-L-alanyl-L-glutaminyl-L-α-aspartyl-L-phenylalanyl-N6-acetyl-L-lysyl-L-threonyl-L-α-aspartyl-L-leucyl-L-arginine, trifluoroacetate salt
Synonyms
  • EIAQDF-K(Ac)-TDLR
  • H-Glu-Ile-Ala-Gln-Asp-Phe-Lys(Ac)-Thr-Asp-Leu-Arg-OH
  • Histone H3 (73-83) (Lys79ac)
  • H3K79Ac
  • [Lys(Ac)79]-Histone H3 (73-83)
Molecular Formula
C60H96N16O21 • XCF3COOH
Formula Weight
Purity
≥95%
A solid
Formic Acid: 1 mg/ml
SMILES
O=C(C)NCCCC[C@@H](C(N[C@]([C@@H](C)O)([H])C(N[C@H](C(N[C@@H](CC(C)C)C(N[C@@H](CCCNC(N)=N)C(O)=O)=O)=O)CC(O)=O)=O)=O)NC([C@@H](NC([C@@H](NC([C@H](CCC(N)=O)NC([C@@H](NC([C@@]([C@H](CC)C)([H])NC([C@H](CCC(O)=O)N[H])=O)=O)C)=O)=O)CC(O)=O)=O)CC1=CC=CC=C1)=O.O=C(O)C(F)(F)F
InChi Code
InChI=1S/C60H96N16O21.C2HF3O2/c1-8-30(4)47(75-50(87)35(61)19-22-44(80)81)57(94)67-31(5)49(86)68-37(20-21-43(62)79)51(88)73-41(27-45(82)83)55(92)72-40(26-34-15-10-9-11-16-34)54(91)69-36(17-12-13-23-65-33(7)78)52(89)76-48(32(6)77)58(95)74-42(28-46(84)85)56(93)71-39(25-29(2)3)53(90)70-38(59(96)97)18-14-24-66-60(63)64;3-2(4,5)1(6)7/h9-11,15-16,29-32,35-42,47-48,77H,8,12-14,17-28,61H2,1-7H3,(H2,62,79)(H,65,78)(H,67,94)(H,68,86)(H,69,91)(H,70,90)(H,71,93)(H,72,92)(H,73,88)(H,74,95)(H,75,87)(H,76,89)(H,80,81)(H,82,83)(H,84,85)(H,96,97)(H4,63,64,66);(H,6,7)/t30-,31-,32+,35-,36-,37-,38-,39-,40-,41-,42-,47-,48-;/m0./s1
InChi Key
PYSKKQCERWNIQQ-SIHMWMQISA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    Product Description

    Histone H3K79Ac (73-83) is a peptide fragment of histone H3 that corresponds to amino acid residues 74-84 of the human histone H3 sequence. Acetylation of histone H3 at lysine 79 has been detected in humans and yeast and is associated with inactive chromatin.1,2,3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Garcia, B.A., Hake, S.B., Diaz, R.L., et alOrganismal differences in post-translational modifications in histones H3 and H4. The Journal of Biological Chemisty 282(10), 7641-7655 (2007).

    2. Bheda, P., Swatkoski, S., Fiedler, K.L., et alBiotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2. Proc. Natl. Acad. Sci. USA 109(16), E916-E925 (2012).

    3. Gatta, R., and Mantovani, R. Single nucleosome ChIPs identify an extensive switch of acetyl marks on cell cycle promoters. Cell Cycle 9(11), 2149-2159 (2010).