Host: E. coli • AA: 339-459 • Tag: N-terminal GST • MW: 42 kDa
Features
  • Due to limited shelf life and/or restricted production, this product is available as custom order only. Please contact our sales office for pricing and lead time.
  • Cayman’s BRD2 bromodomain 2 TR-FRET Assay Kit (Item No. 600510) was developed using BRD2 bromodomain 2 (human recombinant; GST-tagged) protein.
  • Bulk sizes available upon request
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BRD2 bromodomain 2 (human, recombinant)

Item No. 11070

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Bromodomain containing protein 2
  • RING3
  • RNF3
Purity
≥95% estimated by SDS-PAGE
Source
Recombinant N-terminal GST-tagged protein expressed in E. coli
Amino Acids
339-459
MW
42 kDa
Formulation (Request formulation change)
50 mM Tris, pH 7.5, with 500 mM sodium chloride, 5% glycerol, and 5 mM β-mercaptoethanol
UniProt Accession №
P25440
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $329

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    1 mg

    $2,139

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    Product Description

    Bromodomain-containing 2 (BRD2) is a transcriptional regulator that is a member of the bromodomain and extra-terminal (BET) family.1 It is ubiquitously expressed and localizes to the nucleus. BRD2 is composed of two N-terminal bromodomains (BD1 and BD2) that bind acetylated lysine on histones, serving to couple histone acetylation marks to the transcriptional regulation of target promoters, and an extra-terminal domain that mediates chromatin interactions.1,2 BRD2 associates with transcription effector and regulator proteins, including RNA polymerase II, histone acetylases and deacetylases, and transcriptional co-activators and co-repressors to form a transcription complex that regulates the expression of genes involved in inflammation and cell proliferation.1,3 BRD2 also binds to the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) envelope (E) protein, a transmembrane protein involved in CoV virion assembly and pathogenesis of the related virus, SARS-CoV.4,5,6 The BD2 bromodomain of BRD2 contains four α-helices that form the binding site for the acetylated histone H4 tail.7 Point mutations of valine 329 (V329A) or asparagine (N382A) in the BD2 bromodomain eliminate BRD2 binding to acetylated histone H4 lysine 12 (H4K12Ac), and a point mutation of tyrosine 427 (Y427F) abolishes the association between BRD2 and STAT3.8,9 Cayman’s BRD2 bromodomain 2 (human, recombinant) protein can be used for ELISA, Western blot (WB), and binding assay applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Taniguchi, Y. The bromodomain and extra-terminal domain (BET) family: Functional anatomy of BET paralogous proteins. Int. J. Mol. Sci. 17(11), E1849 (2016).

    2. Hnilicová, J., Hozeifi, S., Stejskalová, E., et al. The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing. Mol. Biol. Cell 24(22), 3557-3568 (2013).

    3. Gilan, O., Rioja, I., Knezevic, K., et al. Selective targeting of BD1 and BD2 of the BET proteins in cancer and immuno-inflammation. Science 368(6489), 387-394 (2020).

    4. Gordon, D.E., Jang, G.M., Bouhaddou, M., et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 583(7816), 459-468 (2020).

    5. Kandeel, M., Ibrahim, A., Fayez, M., et al. From SARS and MERS CoVs to SARS-CoV-2: Moving toward more biased codon usage in viral structural and nonstructural genes. J. Med. Virol. 92(6), 660-666 (2020).

    6. Schoeman, D., and Fielding, B.C. Coronavirus envelope protein: Current knowledge. Virol. J. 16(1), 69 (2019).

    7. Umehara, T., Nakamura, Y., Wakamori, M., et al. Structural implications for K5/K12-di-acetylated histone H4 recognition by the second bromodomain of BRD2. FEBS Lett. 584(18), 3901-3908 (2010).

    8. Huang, H., Zhang, J., Shen, W., et al. Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails. BMC Struct. Biol. 7, 57 (2007).

    9. Cheung, K.L., Zhang, F., Jaganathan, A., et al. Distinct roles of Brd2 and Brd4 in potentiating the transcriptional program for Th17 cell differentiation. Mol. Cell 65(6), 1068-1080 (2017).