Cell Signaling Technology

Product Pathways - Jak/Stat Pathway

Stat1 Antibody #9172

Applications Reactivity MW (kDa) Source
W IP H M R Mk (B) 84, 91 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  B=Bovine
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Stat1 Antibody detects endogenous levels of total Stat1 protein. The antibody detects both Stat1alpha (91kDa) and Stat1beta (84 kDa) isoforms.

Source / Purification

Antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to the sequence of human Stat1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from SK-MEL-28 cells, untreated or IFN-alpha-treated (100 ng/ml), using Phospho-Stat1 (Tyr701) Antibody #9171 (upper) or Stat1 Antibody (lower).

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.

  1. Heim, M.H. (1999) J. Recept. Signal. Transduct. Res. 19, 75-120.
  2. Durbin, J.E. et al. (1996) Cell 84, 443-450.
  3. Meraz, M.A. et al. (1996) Cell 84, 431-442.
  4. Ihle, J.N. et al. (1994) Trends Biochem. Sci. 19, 222-227.
  5. Frank, D.A. (1999) Mol. Med. 5, 432-456.
  6. Wen, Z. et al. (1995) Cell 82, 241-250.

Application References

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