Biotinylated Histone Octamer (H3.1)
<strong>Biotinylated Histone Octamer (H3.1) </strong>_x000D_ <strong>Catalog number:</strong> B2016653_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 25 µg_x000D_ <strong>Molecular Weight or Concentration:</strong> 110 kDa_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -80°C_x000D_ <strong>Keywords:</strong> Recombinant Histone Octamer (H3.1) - Biotinylated_x000D_ <strong>Grade:</strong> 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._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Singh MP, Wijeratne SS, Zempleni J. Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation Arch Biochem Biophys. 2013 Jan 15;529(2):105-11._x000D_ 2: Zinchenko A, Berezhnoy NV, Wang S, Rosencrans WM, Korolev N, van der Maarel JRC, Nordenskiöld L. Single-molecule compaction of megabase-long chromatin molecules by multivalent cations Nucleic Acids Res. 2018 Jan 25;46(2):635-649._x000D_ 3: Horn PJ, Crowley KA, Carruthers LM, Hansen JC, Peterson CL. The SIN domain of the histone octamer is essential for intramolecular folding of nucleosomal arrays Nat Struct Biol. 2002 Mar;9(3):167-71._x000D_ 4: Kim KP, Choi J, Yoon J, Bruder JM, Shin B, Kim J, Arauzo-Bravo MJ, Han D, Wu G, Han DW, Kim J, Cramer P, Schöler HR. Permissive epigenomes endow reprogramming competence to transcriptional regulators Nat Chem Biol. 2021 Jan;17(1):47-56._x000D_ 5: Koh-Stenta X, Joy J, Poulsen A, Li R, Tan Y, Shim Y, Min JH, Wu L, Ngo A, Peng J, Seetoh WG, Cao J, Wee JL, Kwek PZ, Hung A, Lakshmanan U, Flotow H, Guccione E, Hill J. Characterization of the histone methyltransferase PRDM9 using biochemical, biophysical and chemical biology techniques Biochem J. 2014 Jul 15;461(2):323-34._x000D_ 6: Al-Ani G, Malik SS, Eastlund A, Briggs K, Fischer CJ. ISWI remodels nucleosomes through a random walk Biochemistry. 2014 Jul 15;53(27):4346-57._x000D_ 7: Di Cerbo V, Mohn F, Ryan DP, Montellier E, Kacem S, Tropberger P, Kallis E, Holzner M, Hoerner L, Feldmann A, Richter FM, Bannister AJ, Mittler G, Michaelis J, Khochbin S, Feil R, Schuebeler D, Owen-Hughes T, Daujat S, Schneider R. Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription Elife. 2014 Mar 25;3:e01632._x000D_ 8: Grigoriev M, Hsieh P. A histone octamer blocks branch migration of a Holliday junction Mol Cell Biol. 1997 Dec;17(12):7139-50._x000D_ 9: Basak R, Rosencrans W, Yadav I, Yan P, Berezhnoy NV, Chen Q, van Kan JA, Nordenskiöld L, Zinchenko A, van der Maarel JRC. Internal Motion of Chromatin Fibers Is Governed by Dynamics of Uncompressed Linker Strands Biophys J. 2020 Dec 1;119(11):2326-2334._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/28126738">10: Koh-Stenta X, Poulsen A, Li R, Wee JL, Kwek PZ, Chew SY, Peng J, Wu L, Guccione E, Joy J, Hill J. Discovery and characterisation of the automethylation properties of PRDM9 Biochem J. 2017 Mar 7;474(6):971-982. </a>_x000D_ _x000D_ <strong>Products Related to Biotinylated Histone Octamer (H3.1) can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>
Product Specifications
Short Description
Catalog Number: B2016653 (25 µg)
Weight
0.15
Length
2
Width
0.5
Height
0.5
Frequently Asked Questions
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