Render Target: STATIC
Render Timestamp:
4/1/2025, 6:42:45 AM EDT
4/1/2025, 10:42:45 AM UTC
Commit: 461ca8d8fe5b1efd4c01fc87e5b5eb592e2d154a
XML generation date: 2025-03-07 13:14:15.109
Product last modified at: 2025-02-21T08:01:00.081Z
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PDP - Template Name: Cell Extracts
PDP - Template ID: *******b5396df

Stat1 Control Cell Extracts #9173

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    Product Information

    Storage

    Supplied in SDS Sample Buffer: 62.5 mM Tris-HCl (pH 6.8 at 25°C), 2% w/v SDS, 10% glycerol, 50 mM DTT, 0.01% w/v bromophenol blue. Store at -20°C. Store at -80°C long term.

    Product Description

    Nonphosphorylated Stat1 Control Cell Extracts: Total cell extracts from HeLa cells prepared without treatment serve as a negative control. Supplied in SDS Sample Buffer.
    Phosphorylated Stat1 Control Cell Extracts: Total cell extracts from HeLa cells prepared with 100 ng/ml interferon-alpha 5 minute treatment serve as a positive control. Supplied in SDS Sample Buffer.

    Background

    The Stat1 transcription factor is activated in response to a large number of ligands (1) and is essential for responsiveness to IFN-α and IFN-γ (2,3). Phosphorylation of Stat1 at Tyr701 induces Stat1 dimerization, nuclear translocation, and DNA binding (4). Stat1 protein exists as a pair of isoforms, Stat1α (91 kDa) and the splice variant Stat1β (84 kDa). In most cells, both isoforms are activated by IFN-α, but only Stat1α is activated by IFN-γ. The inappropriate activation of Stat1 occurs in many tumors (5). In addition to tyrosine phosphorylation, Stat1 is also phosphorylated at Ser727 through a p38 mitogen-activated protein kinase (MAPK)-dependent pathway in response to IFN-α and other cellular stresses (6). Serine phosphorylation may be required for the maximal induction of Stat1-mediated gene activation.
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