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Signal Transducer and Activator of Transcription 1
The His-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns. The purified STAT1 is greater than 90% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 1 unit is the amount sufficient for a gel mobility shift assay in a 20 µl reaction; 100 units are sufficient for a protein-protein interaction assay detected by immuno-blot system.
STAT1 can be used for gel mobility shift assay, for protein-protein and small molecules-protein interactions assay. For research use only.
The protein is in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol. Stored at -70°C before use. Avoid repeated freeze thaw cycles.
MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV SFATIRFHDL
LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIIYSCLK EERKILENAQ
RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR
EHETNGVAKS DQKQEQLLLK KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK
RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV
LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV
KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGTRTN
EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE
PRNLSFFLTP PCARWAQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT
RFCKENINDK NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP
ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EVHPSRLQTT
DNLLPMSPEE FDEVSRIVGS VEFDSMMNTV
Signal transducer and activator of transcription (STAT) proteins are a family of latent cytoplasmic transcription factors involved in cytokine, hormone, and growth factor signal transduction (1). Seven members of the STAT family of transcription factors have been identified in mammalian cells: STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, and STAT6. STAT proteins mediate broadly diverse biologic processes, including cell growth, differentiation, apoptosis, fetal development, transformation, inflammation, and immune response (reviewed in 2, 3). Receptor-recruited STATs are phosphorylated on a single tyrosine residue in the carboxy terminal portion. The modified STATs are released from the cytoplasmic region of the receptor subunits to form homodimers or heterodimers through reciprocal interaction between the phosphotyrosine of one STAT and the SH2 domain of another (4-6). Following dimerization, STATs rapidly translocate to the nucleus and interact with specific regulatory elements to induce target gene transcription (7, 8). Recently, STAT-1 has been implicated in modulating pro- and anti-apoptotic genes following several stress-induced responses. These effects are dependent on STAT-1 phosphorylation on serine-727 and require the C-terminal transactivation domain of STAT-1 to enhance its pro-apoptotic effect or inhibit its anti-apoptotic effects. The STAT-1 C-terminal domain has been demonstrated to be important for protein-protein interaction with other transcriptional activators. The reports that STAT-1-deficient mice develop spontaneous and chemically induced tumours more rapidly compared to wild-type mice and that STAT-1-deficient cells are more resistant to agents that induce apoptosis strongly support the argument that STAT-1 acts as a tumour suppressor.(9)
1. Darnell JE, Kerr IM, Stark GR.Science. 1994; 264:1415-1421
2. Levy, D.E., and J.E. Darnell Jr. 2002. Nat. Rev. Mol. Cell Biol.3:651–662
3. Takeda K, Akira S. Cytokine Growth Factor Rev. 2000; 11:199-207
4. Heldin CH. Cell.1995;80:213-223
5. Bromberg JF. Bioessays. 2001;23:161-169
6. Shuai K, et al. Science. 1993;261:1744-1746
7. Wells JA, et al. Annu Rev Biochem. 1996;65:609-634
8. Darnell JE Jr. Science. 1997;277:1630-1635
9. Stephanou A et al.Int J Exp Pathol. 2003 Dec;84(6):239-44.
This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.
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