Render Target: STATIC
Render Timestamp: 2024-11-21T12:41:41.419Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-09-30 01:53:24.336
Product last modified at: 2024-11-13T13:45:12.453Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

PRMT4/CARM1 (3H2) Mouse mAb #12495

Filter:
  • WB
  • IP
  • IF

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 63
    Source/Isotype Mouse IgG1
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunofluorescence (Immunocytochemistry) 1:50 - 1:200

    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

    PRMT4/CARM1 (3H2) Mouse mAb recognizes endogenous levels of total PRMT4/CARM1 protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the human CARM1 protein.

    Background

    Protein arginine N-methyltransferase 1 (PRMT1) 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, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins (4-6). In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4 (6), components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle (7), the RNA binding protein Sam68 (8), interleukin enhancer-binding factor 3 (ILF3) (9) and interferon-α and β receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PRMT1 isoforms that differ in their amino-terminal regions (11). PRMT1 is localized to the nucleus or cytoplasm, depending on cell type (12,13), and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity (9,14).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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