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rabbit anti-STAT1 (phospho-Tyr701) polyclonal antibody 4797

$366.00

Antibody summary

  • Rabbit polyclonal to STAT1 (phospho-Tyr701)
  • Suitable for: WB,IHC
  • Isotype: Whole IgG
  • 100 µl
SKU: 4797parent Category: Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
host

rabbit

isotype

IgG

clonality

polyclonal

concentration

1 mg/mL

applications

ICC/IF, WB

reactivity

STAT1 (phospho-Tyr701)

available sizes

100 µL

Available product – rabbit anti-STAT1 (phospho-Tyr701) polyclonal antibody 4797

antibody
Tested applications
WB,IHC,IHC
Recommended dilutions
Immunoblotting: use at dilution of 1:500-1:1,000. A band of ~91kDa is detected.

Immunohistochemistry: use at dilution of 1:50-1:100.

These are recommended working dilutions.

End user should determine optimal dilutions for their applications.
Immunogen
Peptide sequence that includes phosphorylation site of tyrosine 701 (T-G-Y(p)-I-K) derived from human STAT1 and conjugated to KLH.
Size and concentration
100µL and 1 mg/mL
Form
liquid
Storage Instructions
This antibody is stable for at least one (1) year at -20°C.
Storage buffer
PBS (without Mg2 and Ca2 ), pH 7.4, 150mM NaCl,
Purity
affinity purified
Clonality
polyclonal
Isotype
IgG
Compatible secondaries
goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863
goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control
Rabbit polyclonal - Isotype Control
target relevance
Protein names
Signal transducer and activator of transcription 1-alpha/beta (Transcription factor ISGF-3 components p91/p84)
Gene names
STAT1,STAT1
Protein family
Transcription factor STAT family
Mass
87335Da
Function
FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors (PubMed:9724754, PubMed:12855578, PubMed:12764129, PubMed:15322115, PubMed:34508746, PubMed:35568036, PubMed:23940278). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus (PubMed:28753426, PubMed:35568036). ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state (PubMed:28753426, PubMed:35568036). In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated (PubMed:26479788). 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 (PubMed:8156998). Becomes activated in response to KITLG/SCF and KIT signaling (PubMed:15526160). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:19088846). Involved in food tolerance in small intestine: associates with the Gasdermin-D, p13 cleavage product (13 kDa GSDMD) and promotes transcription of CIITA, inducing type 1 regulatory T (Tr1) cells in upper small intestine (By similarity). {ECO:0000250|UniProtKB:P42225, ECO:0000269|PubMed:12764129, ECO:0000269|PubMed:12855578, ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:23940278, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28753426, ECO:0000269|PubMed:34508746, ECO:0000269|PubMed:35568036, ECO:0000269|PubMed:8156998, ECO:0000269|PubMed:9724754, ECO:0000303|PubMed:15526160}.
Subellular location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28753426}. Nucleus {ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28753426}. Note=Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4 (PubMed:15322115). Monomethylation at Lys-525 is required for phosphorylation at Tyr-701 and translocation into the nucleus (PubMed:28753426). Translocates into the nucleus in response to interferon-beta stimulation (PubMed:26479788). {ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28753426}.
Structure
SUBUNIT: Isoform alpha homodimerizes upon IFN-gamma induced phosphorylation (PubMed:8605877, PubMed:28753426). Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation (PubMed:8605877). The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9 (By similarity). Interacts (phosphorylated at Ser-727) with PIAS1; the interaction results in release of STAT1 from its target gene (PubMed:9724754, PubMed:17897103). Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466' (PubMed:9121453). Interacts with IFNAR2 (PubMed:9121453). Found in a complex with NMI and CREBBP/CBP (PubMed:9989503). Interacts with NMI which is required for CREBBP/CBP recruitment to the complex (PubMed:9989503). Interacts with PTK2/FAK1 (PubMed:11278462). Interacts with SRC (By similarity). Interacts with ERBB4 (phosphorylated) (PubMed:18721752). Interacts with PARP9 and DTX3L independently of IFN-beta or IFN-gamma-mediated STAT1 'Tyr-701' phosphorylation (PubMed:26479788). Interacts with histone acetyltransferase EP300/p300 in response to INF-gamma stimulation (PubMed:16257975, PubMed:26479788). Interacts with OTOP1 (By similarity). Interacts with IFNGR1 (PubMed:8156998). Interacts with STAT4 (PubMed:34508746). {ECO:0000250|UniProtKB:P42225, ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:16257975, ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:18721752, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28753426, ECO:0000269|PubMed:34508746, ECO:0000269|PubMed:8156998, ECO:0000269|PubMed:8605877, ECO:0000269|PubMed:9121453, ECO:0000269|PubMed:9724754, ECO:0000269|PubMed:9989503}.; SUBUNIT: (Microbial infection) Interacts with Sendai virus C', C, Y1 and Y2 proteins, preventing activation of ISRE and GAS promoter. {ECO:0000269|PubMed:11442634}.; SUBUNIT: (Microbial infection) Interacts with Nipah virus P, V and W proteins preventing activation of ISRE and GAS promoter. {ECO:0000269|PubMed:15140960}.; SUBUNIT: (Microbial infection) Interacts with Rabies virus phosphoprotein preventing activation of ISRE and GAS promoter. {ECO:0000269|PubMed:11442634, ECO:0000269|PubMed:15140960}.; SUBUNIT: (Microbial infection) Interacts with HCV core protein; the interaction results in STAT1 degradation. {ECO:0000269|PubMed:15825084}.; SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP24. {ECO:0000269|PubMed:22383882}.; SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus (EBV) tegument protein BGLF2; this interaction leads to STAT1 dephosphorylation and inhibition. {ECO:0000269|PubMed:34319780}.
Post-translational modification
PTM: Deubiquitinated by USP13; leading to STAT1 stabilization and positive regulation of type I and type II IFN signalings. {ECO:0000269|PubMed:23940278}.; PTM: Phosphorylated on tyrosine and serine residues in response to a variety of cytokines/growth hormones including IFN-alpha, IFN-gamma, PDGF and EGF (PubMed:28753426, PubMed:26479788). Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus (PubMed:21135090). Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent translocation to the nucleus (PubMed:7657660, PubMed:28753426). Growth hormone (GH) activates STAT1 signaling only via JAK2 (PubMed:7657660). Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:17561467, PubMed:19088846). Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2, CAMK2/CAMKII and CK2 in response to IFN-gamma stimulation, is required for maximal transcriptional activity (PubMed:7543024, PubMed:15322115, PubMed:16799645, PubMed:17897103). Phosphorylated on Ser-727 by CAMK2/CAMKII in response to IFN-gamma stimulation and calcium mobilization, promoting activity (PubMed:11972023, PubMed:16257975). Phosphorylated by CAMK2/CAMKII in response to IFN-beta stimulation and calcium mobilization in epithelial cells, promoting activity (PubMed:35568036). Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS (PubMed:17897103). Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents (PubMed:15322115). Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most likely this is catalyzed by a SRC family kinase (PubMed:11278462). Dephosphorylation on tyrosine residues by PTPN2 negatively regulates interferon-mediated signaling (PubMed:12138178). Upon viral infection or IFN induction, phosphorylation on Ser-708 occurs much later than phosphorylation on Tyr-701 and is required for the binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes IKBKE-dependent (PubMed:22065572). Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701 (PubMed:22065572). {ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11972023, ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:16257975, ECO:0000269|PubMed:16799645, ECO:0000269|PubMed:17561467, ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28753426, ECO:0000269|PubMed:35568036, ECO:0000269|PubMed:7543024, ECO:0000269|PubMed:7657660}.; PTM: Sumoylated with 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. {ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:7543024}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-ribosylation prevents phosphorylation at Tyr-701 (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question and the lack of phosphorylation may be due to sumoylation of Lys-703 (PubMed:29858569). {ECO:0000269|PubMed:27796300, ECO:0000305|PubMed:29858569}.; PTM: Monomethylated at Lys-525 by SETD2; monomethylation is necessary for phosphorylation at Tyr-701, translocation into the nucleus and activation of the antiviral defense. {ECO:0000269|PubMed:28753426}.; PTM: (Microbial infection) Ubiquitinated by Herpes simplex virus 2 E3 ubiquitin ligase ICP22. {ECO:0000269|PubMed:32699158}.
Target Relevance information above includes information from UniProt accession : P42224
The UniProt Consortium

Data

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Publications

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Western blot
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