PEG10-RF1 Antibody #93531
Filter:
- WB
Supporting Data
REACTIVITY | H M R |
SENSITIVITY | Endogenous |
MW (kDa) | 50-60 |
SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
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-RF1 Antibody recognizes endogenous levels of total PEG10-RF1 protein. This antibody does not cross-react with PEG10-RF1/RF2. A weak non-specific band has been observed at around 70 kDa in human cell lines.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu325 of human PEG10-RF1 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).
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For Research Use Only. Not For Use In Diagnostic Procedures.
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