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Render Timestamp: 2024-08-14T10:20:19.902Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

PEG10 Antibody #77111

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 50-60, 110
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    PEG10 Antibody recognizes endogenous levels of total PEG10 protein. This antibody detects both RF1 and RF1/RF2.


    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys85 of human PEG10 protein. Antibodies are purified by peptide affinity chromatography.

    Background

    PEG10 (paternally expressed gene 10) is an imprinted gene thought to be derived from a Ty3/Gypsy long terminal repeat (LTR) retrotransposon family encoding Gag- and Pol-like domains (1). Deletion of PEG10 in mice leads to embryonic lethality due to defects in placental formation (2). Similarly, PEG10 deficient trophoblast stem cells exhibited impaired differentiation into placental lineages (3). PEG10 is aberrantly expressed in several cancer types, including hepatocellular carcinoma, and contributes to tumorigenesis by affecting cell proliferation, apoptosis, and metastasis (4). The PEG10 gene has two overlapping open reading frames that are regulated by the programmed process of -1 frameshifting (5). The first encoded protein, ORF1 (or RF1), has a Gag domain with coiled-coil domain and zinc finger domains, while ORF1-2 (or RF1/RF2) is produced by -1 frameshifting and creates a fusion of the ORF1 Gag domain with a carboxyl-terminal Pol-like protease domain. PEG10 has retained the ability to form virus-like particles (VLPs) that are secreted as small extracellular vesicles delivered to distant sites (6). Studies have also shown that PEG10 can bind to mRNA and that PEG10 mRNA can be incorporated into VLPs formed by the PEG10 protein (3,6). Those discoveries have led to a potentially new technique in which unrelated genes can be modified with a region from the PEG10 untranslated region (UTR), allowing genes of interest to be delivered via secreted vesicles (6).

    For Research Use Only. Not For Use In Diagnostic Procedures.
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