Render Target: STATIC
Render Timestamp: 2024-12-20T12:01:04.169Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-10-15 21:38:10.138
Product last modified at: 2024-12-17T19:02:18.332Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

PRMT8 (E2R7O) Rabbit mAb #83283

Filter:
  • WB

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 45
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PRMT8 (E2R7O) Rabbit mAb recognizes endogenous levels of total PRMT8 protein. This antibody does not recognize PRMT1.

    Species Reactivity:

    Mouse

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly323 of human PRMT8 protein.

    Background

    Arginine methylation is a prevalent PTM found on both nuclear and cytoplasmic proteins. Arginine methylated proteins are involved in many different cellular processes, including transcriptional regulation, signal transduction, RNA metabolism, and DNA damage repair (1-3). Arginine methylation is carried out by the arginine N-methyltransferase (PRMT) family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (4). There are three different types of arginine methylation: asymmetric dimethylarginine (aDMA, omega-NG,NG-dimethylarginine), where two methyl groups are placed on one of the terminal nitrogen atoms of the guanidine group of arginine; symmetric dimethylarginine (sDMA, omega-NG,NG-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-methylarginine), where a single methyl group is placed on one of the terminal nitrogen atoms of arginine. Each of these modifications has potentially different functional consequences. Though all PRMT proteins catalyze the formation of MMA, Type I PRMTs (PRMT1, 3, 4, 6, and 8) add an additional methyl group to produce aDMA, while Type II PRMTs (PRMT5 and 7) produce sDMA. Methylated arginine residues often reside in glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (5). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within proline-glycine-methionine rich (PGM) motifs (6).

    PRMT8 is a Type I PRMT closely related to PRMT1 and is expressed primarily in the brain. PRMT8 has a unique N-terminus that is myristoylated, which targets it to the plasma membrane (7). The N-terminal domain also is responsible for PRMT8 activity, and contains two automethylation sites that regulate affinity for AdoMet. (8,9). PRMT8 has been shown to be critical in neural development (10,11). In post-mitotic neurons, PRMT8 provides a protective role against double-stranded DNA breaks that accumulate with aging (12). Overexpression of PRMT8 has been shown to be associated with tau phosphorylation and neuroinflammation (13). PRMT8 is also expressed in stem cells and can control pluripotency and mesodermal fate through the PI3K/Akt/Sox2 axis (14,15).
    1. Bedford, M.T. and Richard, S. (2005) Mol Cell 18, 263-72.
    2. Pahlich, S. et al. (2006) Biochim Biophys Acta 1764, 1890-903.
    3. Bedford, M.T. and Clarke, S.G. (2009) Mol Cell 33, 1-13.
    4. McBride, A.E. and Silver, P.A. (2001) Cell 106, 5-8.
    5. Gary, J.D. and Clarke, S. (1998) Prog Nucleic Acid Res Mol Biol 61, 65-131.
    6. Cheng, D. et al. (2007) Mol Cell 25, 71-83.
    7. Lee, J. et al. (2005) J Biol Chem 280, 32890-6.
    8. Sayegh, J. et al. (2007) J Biol Chem 282, 36444-53.
    9. Dillon, M.B. et al. (2013) J Biol Chem 288, 27872-80.
    10. Lin, Y.L. et al. (2013) PLoS One 8, e55221.
    11. Simandi, Z. et al. (2015) Stem Cells 33, 726-41.
    12. Simandi, Z. et al. (2018) J Neurosci 38, 7683-7700.
    13. Ishii, A. et al. (2022) J Biochem 172, 233-243.
    14. Solari, C. et al. (2016) Biochem Biophys Res Commun 473, 194-199.
    15. Jeong, H.C. et al. (2017) Stem Cells 35, 2037-2049.
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