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Recombinant Human DOT1L/KMT4 Protein

Uniprot : Q8TEK3
  • Cat.No.:PKSH031093

  • Expression host: E.coli

To Purchase PKSH031093

Size:
  • 50μg
Price: $732
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Description

Synonyms DOT1;KMT4
Species Human
Expression_host E.coli
Sequence Gly 2-Lys 416
Accession NP_115871.1
Mol_Mass 47.6 kDa
AP_Mol_Mass 50 kDa
Tag None

Properties

Purity > 90 % as determined by reducing SDS-PAGE.
Endotoxin level Please contact us for more information.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile 20mM HEPES, 150mM NaCl, 1mM EDTA, 15% glycerol, pH 7.5
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed
Reconstitution Please refer to the printed manual for detailed information.

Background

Histone-lysine N-methyltransferase, H3 lysine-79 specific, also known as Histone H3-K79 methyltransferase, DOT1-like protein, Lysine N-methyltransferase 4 and DOT1L, is a nucleus protein which belongs to theDOT1 family. In contrast to other lysine histone methyltransferase, DOT1L does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones. DOT1L is an histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. DOT1L binds to DNA. Methylation of lysine 79 on histone H3 (H3K79) is mediated by DOT1L. It is involved in the regulation of telomeric silencing, development, cell cycle checkpoint and transcription. Mass spectrometry of the DOT1L-containing complex revealed that AF9, ENL and NPM1 were shown to be major DOT1L-interacting proteins. DOT1L might control AF9- and ENL-mediated transcription, regulate RNA processing, and function as a histone chaperone in a NPM1-dependent manner.

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