Render Target: STATIC
Render Timestamp:
6/18/2026, 6:58:50 AM EDT
6/18/2026, 10:58:50 AM UTC
Commit: a854f3e2d877b833e27badd637de63a8a4794b83
XML generation date: 2026-06-17 15:45:40.727
Product last modified at: 2026-06-18T07:01:19.727Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

PRMT5 Antibody #2252

Filter:
  • WB

    Product Specifications

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 73
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    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 and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PRMT5 Antibody detects endogenous levels of total PRMT5 protein. This antibody does not cross-react with other related PRMT proteins.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding amino acid 100 of human PRMT5. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Protein arginine N-methyltransferase 5 (PRMT5) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine, while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT5 and PRMT4/CARM1 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3).

    PRMT5 is the predominant Type II PRMT and was first identified through interaction with Jak2 (4). It can catalyze the symmetric di-methylation of histone H2A and H4 on arginine 3 and histone H3 on arginine 2 and 8 (5-6). Methylation of H2A and H4 is thought to be inactivating through the recruitment of DNA methyltransferases, while methylation of H3 recruits WDR5 and MLL, thus promoting the maintenance of euchromatin (5,7). Other putative roles for PRMT5 have been shown in development, mRNA splicing, and chromatin remodeling (8-10). PRMT5 has been shown to be overexpressed in many different types of cancers (11-14).

    Alternate Names

    72 kDa ICln-binding protein; ANM5; Histone-arginine N-methyltransferase PRMT5; HMT1 hnRNP methyltransferase-like 5; HRMT1L5; HSL7; IBP72; Jak-binding protein 1; JBP1; PRMT5; protein arginine methyltransferase 5; Protein arginine N-methyltransferase 5; Protein arginine N-methyltransferase 5, N-terminally processed; Shk1 kinase-binding protein 1 homolog; SKB1; SKB1 homolog; SKB1Hs

    For Research Use Only. Not for Use in Diagnostic Procedures.
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