Render Target: STATIC
Render Timestamp: 2024-10-11T09:41:48.990Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-09-30 01:57:43.637
Product last modified at: 2024-09-30T08:01:44.642Z
1% for the planet logo
PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

MLL2/KMT2B (E3M1V) Rabbit mAb (Amino-terminal Antigen) #47097

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 320
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    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

    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

    MLL2/KMT2B (E3M1V) Rabbit mAb (Amino-terminal Antigen) recognizes endogenous levels of total MLL2/KMT2B protein. This antibody detects the Taspase 1-cleaved 320 kDa N-terminal MLL2/KMT2B protein (MLL2/KMT2B-N) and the full-length 400 kDa MLL2/KMT2B protein (MLL2/KMT2B-FL).

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala480 of human MLL2/KMT2B protein.

    Background

    The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, mammals contain six Set1-related proteins: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1, and DPY30, which are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6).
    MLL2, also known as histone-lysine N-methyltransferase 2B (KMT2B), functions to activate gene expression by mediating tri-methylation of histone H3 lysine 4 at the promoters of genes involved in embryogenesis and hematopoiesis, and is required for histone H3 lysine 4 tri-methylation at bivalent promoters in embryonic stem cells (7). Like MLL1, MLL2 is a large protein made up of approximately 2,700 amino acids that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL2-N) and C-terminal (MLL2-C) fragments, both of which are subunits of the functional MLL2/COMPASS complex. MLL2-N, MLL2-C, WDR5, RBBP5, and ASH2L define the core catalytic component of the MLL2/COMPASS complex, which is recruited to target genes to regulate transcription. MLL1 gene translocations are often associated with various hematological malignancies and thought to be a driving component of these types of leukemia. MLL2 is required for memory formation, proper glucose homeostasis, and cardiac lineage differentiation of mouse embryonic stem cells (8-11). A recent study has shown that MLL2 is required for survival of MLL-AF9-transformed cells, implicating MLL2 as a potential modulator of MLL1-rearranged leukemias (12). Mutations in MLL2 cause complex early-onset dystonia, and overexpression of MLL2 is associated with gastrointestinal diffuse large B-cell lymphoma (13,14).
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    XP is a registered trademark of Cell Signaling Technology, Inc.
    All other trademarks are the property of their respective owners. Visit our Trademark Information page.