| Weight | 1 lbs |
|---|---|
| Dimensions | 9 × 5 × 2 in |
| host | rabbit |
| isotype | IgG |
| clonality | polyclonal |
| concentration | 1 mg/mL |
| applications | ICC/IF, WB |
| reactivity | STAT3 (phospho-Ser727) |
| available sizes | 100 µL |
rabbit anti-STAT3 (phospho-Ser727) polyclonal antibody 8081
$366.00
Antibody summary
- Rabbit polyclonal to STAT3 (phospho-Ser727)
- Suitable for: WB,IHC,IF
- Isotype: Whole IgG
- 100 µl
rabbit anti-STAT3 (phospho-Ser727) polyclonal antibody 8081
| antibody |
|---|
| Tested applications WB,IHC,IHC,ICC/IF |
| Recommended dilutions Immunoblotting: use at dilution of 1:500-1:1,000. A band of ~88kDa is detected. Immunohistochemistry: use at dilution of 1:50-1:100. Immunofluorescence: use at dilution of 1:100-1:200. These are recommended working dilutions. End user should determine optimal dilution |
| Immunogen Peptide sequence that includes phosphorylation site of Serine 727 (P-M-S(p)-P-R) derived from human STAT3 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 3 (Acute-phase response factor) |
| Gene names STAT3,STAT3 APRF |
| Protein family Transcription factor STAT family |
| Mass 88068Da |
| Function FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:10688651, PubMed:12359225, PubMed:12873986, PubMed:15194700, PubMed:17344214, PubMed:18242580, PubMed:22306293, PubMed:23084476, PubMed:32929201). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:17344214, PubMed:32929201). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:12873986). Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes (PubMed:12359225). Activated by IL31 through IL31RA (PubMed:15194700). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (PubMed:28065600). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (PubMed:23084476). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity). {ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12359225, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:32929201}. |
| Subellular location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:31899195}. Nucleus {ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:31899195}. Note=Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1. |
| Tissues TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in naive CD4(+) T cells as well as T-helper Th17, Th1 and Th2 cells (PubMed:31899195). {ECO:0000269|PubMed:31899195}. |
| Structure SUBUNIT: Forms a homodimer or a heterodimer with a related family member (at least STAT1) (PubMed:28065600). Interacts with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1 (PubMed:15994929, PubMed:15194700, PubMed:17344214, PubMed:15677474, PubMed:15467733) (By similarity). Interacts with IL23R in presence of IL23 (PubMed:12023369). Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the interaction is enhanced by LIF and JAK1 expression (By similarity). Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of nuclear import (By similarity). Interacts with CAV2; the interaction is increased on insulin-induced tyrosine phosphorylation of CAV2 and leads to STAT3 activation (By similarity). Interacts with ARL2BP; interaction is enhanced with ARL2 (PubMed:18234692). Interacts with NEK6 (By similarity). Binds to CDK9 when activated and nuclear (PubMed:17956865). Interacts with BMX (PubMed:10688651). Interacts with ZIPK/DAPK3 (PubMed:16219639). Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3 (PubMed:9388184). In prostate cancer cells, interacts with PRKCE and promotes DNA binding activity of STAT3 (PubMed:17875724). Interacts with STMN3, antagonizing its microtubule-destabilizing activity (By similarity). Interacts with the 'Lys-129' acetylated form of BIRC5/survivin (PubMed:20826784). Interacts with FER (PubMed:19147545). Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain) (PubMed:23084476). Interacts with INPP5F; the interaction is independent of STAT3 Tyr-705 phosphorylation status (PubMed:25476455). Interacts with FGFR4 (PubMed:26675719). Interacts with OCAD1 (By similarity). Interacts (unphosphorylated or phosphorylated at Ser-727) with PHB1 (PubMed:31899195). Interacts and may form heterodimers with NHLH1 (By similarity). Found in a complex with SLC39A6, SLC39A10 and with the 'Ser-727' phosphorylated form of STAT3 throughout mitosis (PubMed:32797246). Interacts (when phosphorylated at Tyr-705) with CD274/PD-L1; promoting nuclear translocation of CD274/PD-L1 (PubMed:32929201). {ECO:0000250|UniProtKB:P42227, ECO:0000250|UniProtKB:P52631, ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:11773079, ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:15994929, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:19147545, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:25476455, ECO:0000269|PubMed:26675719, ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:31899195, ECO:0000269|PubMed:32797246, ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:9388184}.; SUBUNIT: (Microbial infection) Interacts with HCV core protein. {ECO:0000269|PubMed:12208879}.; SUBUNIT: (Microbial infection) Interacts with S.typhimurium SarA. {ECO:0000269|PubMed:29924996}.; SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus (HHV-5) immediate early protein IE1; this interaction leads to STAT3 nuclear accumulation and disruption of IL6-induced STAT3 phosphorylation. {ECO:0000269|PubMed:27387064}. |
| Post-translational modification PTM: Tyrosine phosphorylated upon stimulation with EGF. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity. ARL2BP may participate in keeping the phosphorylated state of STAT3 within the nucleus. Upon LPS challenge, phosphorylated within the nucleus by IRAK1. Upon erythropoietin treatment, phosphorylated on Ser-727 by RPS6KA5. Phosphorylation at Tyr-705 by PTK6, isoform M2 of PKM (PKM2) or FER leads to an increase of its transcriptional activity (PubMed:12763138, PubMed:16568091, PubMed:21135090, PubMed:22306293, PubMed:32929201). Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling. {ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12359225, ECO:0000269|PubMed:12763138, ECO:0000269|PubMed:15465816, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:16568091, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19147545, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:7701321}.; PTM: Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (PubMed:28065600). {ECO:0000269|PubMed:28065600}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (PubMed:28065600). {ECO:0000269|PubMed:28065600}.; PTM: (Microbial infection) Phosphorylated on Tyr-705 in the presence of S.typhimurium SarA. {ECO:0000269|PubMed:29924996}. |
| Target Relevance information above includes information from UniProt accession : P40763 |
| The UniProt Consortium |
Data
| No results found |
Publications
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Protocols
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| Western blot IHC ICC |
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