Render Target: STATIC
Render Timestamp: 2024-10-31T10:42:53.987Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-09-30 01:55:18.281
Product last modified at: 2024-09-30T08:01:23.973Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

THEX1 (D2B4) Rabbit mAb #4052

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 46
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    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

    THEX1 (D2B4) Rabbit mAb detects endogenous levels of total THEX1 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the sequence around Gly338 of human THEX1.

    Background

    THEX1 (3’hExo) is a 3’ exonuclease that may play a role in the degradation of histone mRNA transcripts (1). A recently identified member of the DEDDh 3' exonuclease family, THEX1 binds the conserved stem-loop structure found at the 3’ end of mRNA in vitro (2). The binding of THEX1 to mRNA requires the presence of a terminal ACCCA sequence and is enhanced by the concurrent binding of stem-loop binding protein (SLBP). Cleavage of histone mRNA by THEX1 exonuclease may help produce the rapid turnover of histone mRNA transcripts associated with the completion of DNA replication (3). Additional evidence suggests that THEX1 may be responsible for excising the remaining few 3’ nucleotides following cleavage by a different enzyme (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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