Overview

  • Product nameAnti-STAT1 antibody [EPYR2154]See all STAT1 primary antibodies ...
  • Description
    Rabbit monoclonal [EPYR2154] to STAT1
  • Tested applicationsWB, IP, Flow Cytmore details
  • Species reactivity
    Reacts with: Mouse, Human

    Does not react with

    Rat
  • Immunogen

    A synthetic peptide corresponding to residues within Human STAT1

  • Positive control
    • HeLa, 293, NIH-3T3 and A431 cell lysates
  • General notes

    Produced under U.S. Patent No. 5,675,063. A 40 μl trial size is available to purchase for this antibody.

Properties

Applications

Our Abpromise guarantee covers the use of ab92506 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB
IP
Flow Cyt
  • Application notesFlow Cyt: 1/50.
    IP: 1/50.
    WB: 1/1000 - 1/2000. Predicted molecular weight: 87 kDa.

    Is unsuitable for ICC or IHC-P.

    Not yet tested in other applications.
    Optimal dilutions/concentrations should be determined by the end user.
  • Target

    • FunctionSignal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.
    • Involvement in diseaseNote=STAT1 deficiency results in impaired immune response leading to severe mycobacterial and viral diseases. In the case of complete deficiency, patients can die of viral disease.
      Defects in STAT1 are a cause of mendelian susceptibility to mycobacterial disease (MSMD) [MIM:209950]; also known as familial disseminated atypical mycobacterial infection. This rare condition confers predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. The pathogenic mechanism underlying MSMD is the impairment of interferon-gamma mediated immunity whose severity determines the clinical outcome. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. MSMD is a genetically heterogeneous disease with autosomal recessive, autosomal dominant or X-linked inheritance.
    • Sequence similaritiesBelongs to the transcription factor STAT family.
      Contains 1 SH2 domain.
    • Post-translational
      modifications
      Phosphorylated on tyrosine and serine residues in response to IFN-alpha, IFN-gamma, PDGF and EGF. Phosphorylation on Tyr-701 (lacking in beta form) by JAK promotes dimerization and subsequent translocation to the nucleus. Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS. Phosphorylation on Ser-727 by PKCdelta induces apoptosis in response to DNA-damaging agents.
      Sumoylated by SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins. Enhances the transactivation activity.
      ISGylated.
    • Cellular localizationCytoplasm. Nucleus. Translocated into the nucleus in response to IFN-gamma-induced tyrosine phosphorylation and dimerization.
    • Information by UniProt
    • Database links
    • Alternative names
      • Signal transducer and activator of transcription 1 91kD antibody
      • CANDF7 antibody
      • DKFZp686B04100 antibody
      • ISGF 3 antibody
      • ISGF-3 antibody
      • OTTHUMP00000163552 antibody
      • OTTHUMP00000165046 antibody
      • OTTHUMP00000165047 antibody
      • OTTHUMP00000205845 antibody
      • Signal transducer and activator of transcription 1 91kD antibody
      • Signal transducer and activator of transcription 1 91kDa antibody
      • Signal transducer and activator of transcription 1 antibody
      • Signal transducer and activator of transcription 1, 91kD antibody
      • Signal transducer and activator of transcription 1-alpha/beta antibody
      • STAT 1 antibody
      • Stat1 antibody
      • STAT1_HUMAN antibody
      • STAT91 antibody
      • Transcription factor ISGF 3 components p91 p84 antibody
      • Transcription factor ISGF-3 components p91/p84 antibody
      see all

    Anti-STAT1 antibody [EPYR2154] images

    • All lanes : Anti-STAT1 antibody [EPYR2154] (ab92506) at 1/1000 dilution

      Lane 1 : HeLa cell lysate
      Lane 2 : 293 cell lysate
      Lane 3 : NIH-3T3 cell lysate
      Lane 4 : A431 cell lysate

      Lysates/proteins at 10 µg per lane.

      Secondary
      HRP labelled goat anti-rabbit IgG at 1/2000 dilution

      Predicted band size : 87 kDa
      Observed band size : 91 kDa (why is the actual band size different from the predicted?)

    References for Anti-STAT1 antibody [EPYR2154] (ab92506)

    This product has been referenced in:
    • Nishizawa K  et al. Efficacy and mechanism of a glycoside compound inhibiting abnormal prion protein formation in prion-infected cells: implications of interferon and phosphodiesterase 4D-interacting protein. J Virol 88:4083-99 (2014). Read more (PubMed: 24453367) »
    • Frolov I  et al. Early events in alphavirus replication determine the outcome of infection. J Virol 86:5055-66 (2012). WB . Read more (PubMed: 22345447) »

    See all 3 Publications for this product

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