1110034C02Rik; Acute Phase Response Factor; Acute-phase response factor; ADMIO; APRF; AW109958; DNA binding protein APRF; FLJ20882; HIES; MGC16063; Signal transducer and activator of transcription 3 (acute phase response factor); Signal transducer and activator of transcription 3; STAT 3; Stat3; STAT3_HUMAN;
WB 1:500-1:2000, IHC 1:50-1:200, IP, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Human, Mouse, Rat
Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(91%), Rabbit(100%), Chicken(100%)
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Phospho-STAT3 (Tyr705) Antibody detects endogenous levels of STAT3 only when phosphorylated at Tyrosine 705.
Please cite this product as: Affinity Biosciences Cat# AF3293, RRID:AB_2810278.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
A synthesized peptide derived from human STAT3 around the phosphorylation site of Tyr705.
Observed Mol.Wt.: 86kD.
Predicted Mol.Wt.: 88kDa(Calculated)..
Cytoplasm. Nucleus. 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.
Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators.
Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. 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. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1. 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. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity).
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 or FER leads to an increase of its transcriptional activity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling.
Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.
Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.
(Microbial infection) Phosphorylated on Tyr-705 in the presence of S.typhimurium SarA.
S-palmitoylated by ZDHHC19 in SH2 putative lipid-binding pockets, leading to homodimerization. Nuclear STAT3 is highly palmitoylated (about 75%) compared with cytoplasmic STAT3 (about 20%).
S-stearoylated, probably by ZDHHC19.
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.
Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
Forms a homodimer or a heterodimer with a related family member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1 (By similarity). Interacts with IL23R in presence of IL23. 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. Interacts with NEK6 (By similarity). Binds to CDK9 when activated and nuclear. Interacts with BMX. Interacts with ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. In prostate cancer cells, interacts with STAT3 and promotes DNA binding activity of STAT3. Interacts with STMN3, antagonizing its microtubule-destabilizing activity. Interacts with the 'Lys-129' acetylated form of BIRC5/survivin. Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with STAT3; the interaction is independent of STAT3 Tyr-705 phosphorylation status. Interacts with FGFR4. Interacts with OCAD1 (By similarity). Interacts with ZDHHC19, leading to palmitoylation which promotes homodimerization and activation.
(Microbial infection) Interacts with HCV core protein.
(Microbial infection) Interacts with S.typhimurium SarA.
Belongs to the transcription factor STAT family.
· Cellular Processes > Cellular community - eukaryotes > Signaling pathways regulating pluripotency of stem cells.(View pathway)
· Cellular Processes > Cell growth and death > Necroptosis.(View pathway)
· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Jak-STAT signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > FoxO signaling pathway.(View pathway)
· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Immune diseases > Inflammatory bowel disease (IBD).
· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.
· Human Diseases > Infectious diseases: Viral > Hepatitis B.
· Human Diseases > Infectious diseases: Viral > Measles.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Human Diseases > Infectious diseases: Viral > Hepatitis C.
· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
· Human Diseases > Cancers: Specific types > Acute myeloid leukemia.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Specific types > Non-small cell lung cancer.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Pancreatic cancer.(View pathway)
· Organismal Systems > Immune system > Chemokine signaling pathway.(View pathway)
· Organismal Systems > Endocrine system > Prolactin signaling pathway.(View pathway)
· Organismal Systems > Immune system > Th17 cell differentiation.(View pathway)
· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.
Application: WB Species:human; Sample:HepG2
Figure 6. Effect of BCL2L10 on its downstream gene expression profiles of human cancer pathway in HepG2 cells. (A) By human cancer pathway PCR array, ectopic expression of BCL2L10 up- or down-regulated several genes related to tumor proliferation, apoptosis, metastasis and angiogenesis. (B) Western blot was performed to confirm the downstream gene expression regulated by BCL2L10 in HepG2 cells. GAPDH was used as an internal control. (C) Schematic diagram of the molecular events for BCL2L10 function as a tumor suppressor through regulating cell cycle, proliferation, apoptosis metastasis and angiogenesis effectors.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
|Y705||Phosphorylation||O60674 (JAK2) , Q15300 (RET/PTC2) , P23458 (JAK1) , P22455 (FGFR4) , P27361 (MAPK3) , Q13882 (PTK6) , P22607 (FGFR3) , Q9UM73 (ALK) , P14618 (PKM) , P16591 (FER) , P12931 (SRC)||Uniprot|
|S727||Phosphorylation||P51812 (RPS6KA3) , P45984-2 (MAPK9) , Q13233 (MAP3K1) , O75582 (RPS6KA5) , P28482 (MAPK1) , Q13555 (CAMK2G) , O43293 (DAPK3) , P42345 (MTOR) , P27361 (MAPK3) , Q02156 (PRKCE) , P45983 (MAPK8) , P51617 (IRAK1) , Q16539 (MAPK14) , Q05655 (PRKCD) , Q9UBE8 (NLK) , P06493 (CDK1) , Q00535 (CDK5) , Q9HC98 (NEK6)||Uniprot|