Host: E. coli • AA: 2-130 • MW: 13.96 kDa
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Histone H2A Type 1 (human, recombinant)

Item No. 11080

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • H2A Clustered Histone 11
  • H2A Histone Family, Member P
  • H2A.1
  • H2AC11
  • H2AFP
  • HIST1H2AG
  • Histone H2A/ptl
Purity
≥90% estimated by SDS-PAGE
Source
Recombinant human histone H2A type 1 expressed in E. coli
Amino Acids
2-130 (full length)
MW
13.96 kDa
Formulation (Request formulation change)
A solution in water
UniProt Accession №
P0C0S8
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    500 µg

    $528

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    Product Description

    Histone H2A type 1 (H2A.1) is a variant of the histone H2A protein that is encoded by H2AC11, previously known as HIST1H2AG, in humans.1 Histone H2A is a core histone that forms a dimer with histone H2B.2 Two histone H2A/H2B dimers form an octameric nucleosome with a histone H3/H4 tetramer, around which DNA wraps, allowing it to be condensed. Histone H2A can be post-translationally modified via methylation of the arginine at position 3 by protein arginine methyltransferase 1 (PRMT1), PRMT5, or PRMT6, which is associated with both transcriptional activation and repression.3 When methylated by PRMT7, it is associated with DNA damage repair. The arginine residue at position 3 of histone H2A is also subject to citrullination by protein arginine deiminase 4 (PAD4). H2A.1 levels are higher in peripheral blood mononuclear cells (PBMCs) isolated from patients with active systemic lupus erythematosus (SLE) compared to those with stable SLE, rheumatoid arthritis (RA), or non-SLE non-RA controls.4 Cayman’s Histone H2A Type 1 (human, recombinant) protein can be used for Western blot and ELISA applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Marzluff, W.F., Gongidi, P., Woods, K.R., et al. The human and mouse replication-dependent histone genes. Genomics 80(5), 487-498 (2002).

    2. Eickbush, T.H., and Moudrianakis, E.N. The histone core complex: An octamer assembled by two sets of protein-protein interactions. Biochemistry 17(23), 4955-4964 (1978).

    3. Fuhrmann, J., and Thompson, P.R. Protein arginine methylation and citrullination in epigenetic regulation. ACS Chem. Biol. 11(3), 654-668 (2016).

    4. Wang, L., Dai, Y., Qi, S., et al. Comparative proteome analysis of peripheral blood mononuclear cells in systemic lupus erythematosus with iTRAQ quantitative proteomics. Rheumatol. Int. 32(3), 585-593 (2012).