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Histone H3 Peptide Substrate

$495.00

Catalog Number: B2013164 (1 mg)
Histone H3 Peptide Substrate is a high quality Histone H3 Peptide Substrate (sequence 1-21). This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

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SKU: B2013164 Categories: , Tag:

Description

Histone H3 Peptide Substrate
Catalog number: B2013164
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1 mg
Molecular Weight or Concentration: 2254.6 g/mol
Supplied as: Lyophilized
Applications: molecular tool for various biochemical applications
Storage: -20°C
Keywords: H3 Peptide
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Mulvaney KM, Blomquist C, Acharya N, Li R, Ranaghan MJ, O’Keefe M, Rodriguez DJ, Young MJ, Kesar D, Pal D, Stokes M, Nelson AJ, Jain SS, Yang A, Mullin-Bernstein Z, Columbus J, Bozal FK, Skepner A, Raymond D, LaRussa S, McKinney DC, Freyzon Y, Baidi Y, Porter D, Aguirre AJ, Ianari A, McMillan B, Sellers WR. Molecular basis for substrate recruitment to the PRMT5 methylosome Mol Cell. 2021 Sep 2;81(17):3481-3495.e7.
2: Merx J, Hintzen JCJ, Proietti G, Elferink H, Wang Y, Porzberg MRB, Sondag D, Bilgin N, Park J, Mecinović J, Boltje TJ. Investigation of in vitro histone H3 glycosylation using H3 tail peptides Sci Rep. 2022 Nov 10;12(1):19251.
3: Cornett EM, Dickson BM, Vaughan RM, Krishnan S, Trievel RC, Strahl BD, Rothbart SB. Substrate Specificity Profiling of Histone-Modifying Enzymes by Peptide Microarray Methods Enzymol. 2016;574:31-52.
4: Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Müller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S. Histone recognition and large-scale structural analysis of the human bromodomain family Cell. 2012 Mar 30;149(1):214-31.
5: Petronikolou N, Longbotham JE, Fujimori DG. Extended Recognition of the Histone H3 Tail by Histone Demethylase KDM5A Biochemistry. 2020 Feb 11;59(5):647-651.
6: Kinney CM, Chandrasekharan UM, Yang L, Shen J, Kinter M, McDermott MS, DiCorleto PE. Histone H3 as a novel substrate for MAP kinase phosphatase-1 Am J Physiol Cell Physiol. 2009 Feb;296(2):C242-9.
7: Elsässer SJ, Huang H, Lewis PW, Chin JW, Allis CD, Patel DJ. DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition Nature. 2012 Nov 22;491(7425):560-5.
8: Proietti G, Wang Y, Punzo C, Mecinović J. Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 Int J Mol Sci. 2021 Jan 15;22(2):846.
9: Patnaik D, Chin HG, Estève PO, Benner J, Jacobsen SE, Pradhan S. Substrate specificity and kinetic mechanism of mammalian G9a histone H3 methyltransferase J Biol Chem. 2004 Dec 17;279(51):53248-58.
10: Longbotham JE, Chio CM, Dharmarajan V, Trnka MJ, Torres IO, Goswami D, Ruiz K, Burlingame AL, Griffin PR, Fujimori DG. Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling Nat Commun. 2019 Jan 9;10(1):94.

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