STAT1 N-terminus, Human Antibody from MILTENYI BIOTEC B.V. & Co. KG

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Antigenic SpecificitySTAT1 N-terminus, Human
CloneREA272
Host SpeciesRecombinant Human
Reactive Specieshuman, mouse, rat, other
IsotypeIgG1
FormatVio B515 conjugate
Size30 tests in 60 µL
Concentration1:50
ApplicationsIntracellular flow cytometry
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DescriptionSTAT1 N-terminus Antibody, anti-human, Vio® B515, REAfinity™. Clone REA272 recognizes the N-terminus of the signal transducer and activator of transcription 1-α/β (STAT1) antigen, regardless of phosphorylation status. STAT1 is expressed in two alternatively spliced isoforms (91 kDa STAT1α and 84 kDa STAT1β) and clone REA272 recognizes both isoforms. STAT1 expression is found ubiquitously. It is involved in upregulating genes due to a signal by either type I, type II, or type III interferons. In response to interferon γ (IFN-γ) stimulation, the STAT1 subunits become tyrosine-phosphorylated at Y701, and the complex is translocated to the nucleus. STAT1 forms homodimers or heterodimers with STAT3 that bind to the IFN-γ activated sequence promoter element. In response to either IFN-α or IFN-β stimulation, STAT1 forms a heterodimer with STAT2 that can bind the interferon stimulated response promoter element. In either case, binding of the promoter element leads to an increased expression of interferon stimulated genes. | Additional information: Clone REA272 displays negligible binding to Fc receptors. |
Immunogenn/a
Other NamesCANDF7, IMD31A, IMD31B, IMD31C, ISGF-3, STAT91
Gene, Accession #Gene ID: 6772
Catalog #130-131-000
Price$158
Order / More InfoSTAT1 N-terminus, Human Antibody from MILTENYI BIOTEC B.V. & Co. KG
Product Specific ReferencesGimeno, R. et al. (1996) STAT1 implication in the immune response to superantigens in vivo. J Immunol 156: 1378-1386. | Sikorski, K. et al. (2011) STAT1-mediated signal integration between IFNγ and LPS leads to increased EC and SMC activation and monocyte adhesion. Am. J. Physiol., Cell Physiol. 300: C1337-C1344. | Mowen, K. et al. (1998) Role of the STAT1-SH2 domain and STAT2 in the activation and nuclear translocation of STAT1. J. Biol. Chem. 273: 30073-30076. | ten Hoeve, J. et al. (2002) Identification of a nuclear Stat1 protein tyrosine phosphatase. Mol. Cell. Biol. 16: 5662-5668.
MILTENYI BIOTEC B.V. & Co. KG
MILTENYI BIOTEC B.V. & Co. KG
MILTENYI BIOTEC B.V. & Co. KG
Friedrich-Ebert-Straße 68
51429 Bergisch Gladbach GERMANY
P: +49 2204 8306-0
F: +49 2204 85197

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