Host: E. coli • AA: 2,438-2,561 (partial protein) • Tag: N-terminal GST • MW: 42 kDa
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ASH1L bromodomain (human, recombinant)

Item No. 14489

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Absent, Small, or Homeotic Discs 1-like
  • ASH1-like, Histone Lysine Methyltransferase Complex Subunit
  • Histone Lysine Methyltransferase Complex Subunit
Purity
≥90% estimated by SDS-PAGE
Source
Recombinant N-terminal GST-tagged protein expressed in E. coli
Amino Acids
2,438-2,561 (partial protein)
MW
42 kDa
Formulation (Request formulation change)
50 mM Tris, pH 8.0, with 150 mM sodium chloride and 20% glycerol
UniProt Accession №
Q9NR48
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    1 mg

    $2,661

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    Product Description

    The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. Acetylated lysine residues are recognized by a small protein domain known as a bromodomain.1 These domains function in linking protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as “readers” of histone acetylation marks regulating the transcription of target promoters.2 ASH1L is the mammalian homolog of the Drosophila protein Absent, small, or homeotic disc 1 (Ash1), a trithorax group histone methyltransferase involved in gene activation.3 ASH1L contains an associated with SET domain, a SET domain, a post-SET domain, a bromodomain, a bromoadjacent homology domain, and a plant homeodomain finger.3,4 ASH1L regulates mammalian Hox gene expression, which plays an important role in haematopoietic development in mammals. ASH1L has been reported to methylate histone H3 at lysine 4 (H3K4) and H3K36.5,6,3 This protein product contains the bromodomain region of ASH1L.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Mujtaba, S., Zeng, L., and Zhou, M.-M. Structure and acetyl-lysine recognition of the bromodomain. Oncogene 26(37), 5521-5527 (2007).

    2. Muller, S., Filippakopoulos, P., and Knapp, S. Bromodomains as therapeutic targets. Expert Rev. Mol. Med. 13, e29 (2011).

    3. An, S., Yeo, K.J., Jeon, Y.H., et al. Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. The Journal of Biological Chemisty 286(10), 8369-8374 (2011).

    4. Nakamura, T., Blechman, J., Tada, S., et al. huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions. Proc. Natl. Acad. Sci. USA 97(13), 7284-7289 (2000).

    5. Tanaka, Y., Kawahashi, K., Katagiri, Z.I., et al. Dual function of histone H3 lysine 36 methyltransferase ASH1 in regulation of Hox gene expression. PLoS One 6(11), (2011).

    6. Gregory, G.D., Vakoc, C.R., Rozovskaia, T., et al. Mammalian ASH1L is a histone methyltransferase that occupies the transcribed region of active genes. Mol. Cell. Biol. 27(24), 8466-8479 (2007).