Peptides

[Lys(Ac)5]-Histone H4 (1-21)-GGK(Biotin) - 1 mg

$291.00
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  • Cat.Number : AS-64844-1
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    In stock

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This peptide is histone H4 amino acids 1 to 21, acetylated at Lys-5 and at the N-terminus. This peptide also contains a C-terminal GG linker, followed by a biotinylated lysine. The acetylation of histone H4 causes structural changes that play a crucial role in amplifying the binding of transcription factors to specific recognition sites within the nucleosome.

Specifications

Chemistry
Sequence one letter code
  • Ac-SGRG-K(Ac)-GGKGLGKGGAKRHRKV-GGK(Biotin)
Sequence three letter code
  • Ac-Ser-Gly-Arg-Gly-Lys(Ac)-Gly-Gly-Lys-Gly-Leu-Gly-Lys-Gly-Gly-Ala-Lys-Arg-His-Arg-Lys-Val-Gly-Gly-Lys(Biotin)-OH
Molecular Mass/ Weight
  • 2644.2
Modification
Conjugation type
  • Biotins
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • human

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Citations

Selective recognition of H3.1K36 dimethylation/H4K16 acetylation facilitates the regulation of all-trans-retinoic acid (ATRA)-responsive genes by putative chromatin reader ZMYND8

J. Biol. Chem. . 2015 Dec 11 ; 291(6) 2664 | DOI : 10.1074/jbc.M115.679985

  • S. Adhikary

Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation.

PNAS . 2014 Mar 10 ; 111(12) E1072 | DOI : 10.1073/pnas.1319122111

  • C. Das

References

Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro

EMBO J . 1996 May 15 ; 15(10) 2508 | DOI : https://doi.org/10.1002/j.1460-2075.1996.tb00608.x

  • M. Vettese-Dadey
  • et al