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Immunohistochemistry analysis of STAT3 [pS727] showing staining in the cytoplasm of paraffin-embedded mouse brain tissue (right) compared to a negative control without primary antibody (left). To expose target proteins, antigen retrieval was performed using 10mM sodium citrate (pH 6.0), microwaved for 8-15 min. Following antigen retrieval, tissues were blocked in 3% H2O2-methanol for 15 min at room temperature, washed with ddH2O and PBS, and then probed with a STAT3 [pS727] Rabbit Polyclonal Antibody (44384G) diluted in 3% BSA-PBS at a dilution of 1:20 overnight at 4°C in a humidified chamber. Tissues were washed extensively in PBST and detection was performed using an HRP-conjugated secondary antibody followed by colorimetric detection using a DAB kit. Tissues were counterstained with hematoxylin and dehydrated with ethanol and xylene to prep for mounting.
|Tested species reactivity||Mouse , Human , Rat|
|Published species reactivity||Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phosphopeptide from human STAT3 containing serine 727. This region is conserved between human, mouse and rat.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 1mg/ml BSA, 50% glycerol|
|Contains||0.05% sodium azide|
|Tested Applications||Dilution *|
|ChIP assay (ChIP)||10µl|
|Immunohistochemistry (Paraffin) (IHC (P))||1:10-1:100|
|Western Blot (WB)||1:200-1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
STATs (signal transducers and activators of transcription) were originally discovered as two proteins (STAT1 and STAT2) which were involved in interferon-alpha (IFN-alpha) and IFN-gamma signal transduction. Since then, several additional STAT proteins have been identified (STAT3, 4, 5a, 5b, and 6). STATs undergo tyrosine phosphorylation in response to growth factor or cytokine signaling. This phosphorylation results in dimerization and translocation of STAT proteins to the nucleus. In some cases this process is mediated by JAK Kinases (Janus Kinases 1, 2, and 3). For maximum activation of these proteins, phosphorylation at specific tyrosine and serine residues may be required in STAT1 alpha, 3, 4, and 5. Specific functions of the various members of the STAT family are poorly understood. STAT3 has been shown to be activated by IFN-alpha but not IFN-beta. The transcription factors associated with STAT3 are c-Jun and cyclic AMP-responsive enhancer binding protein (CREB). Deletion of the STAT3 gene in knock-out mice was lethal at the early embryonic stage.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Early-onset and robust amyloid pathology in a new homozygous mouse model of Alzheimer's disease.
||Willuweit A,Velden J,Godemann R,Manook A,Jetzek F,Tintrup H,Kauselmann G,Zevnik B,Henriksen G,Drzezga A,Pohlner J,Schoor M,Kemp JA,von der Kammer H||PloS one (4:null)||2009|
Melanocortin potentiates leptin-induced STAT3 signaling via MAPK pathway.
44-384G was used in western blot to study interactions between leptin and alpha-melanocyte stimulating hormone signaling.
|Zhang Y,Wu X,He Y,Kastin AJ,Hsuchou H,Rosenblum CI,Pan W||Journal of neurochemistry (110:390)||2009|
Protein tyrosine phosphatase 1B negatively regulates leptin signaling in a hypothalamic cell line.
||Kaszubska W,Falls HD,Schaefer VG,Haasch D,Frost L,Hessler P,Kroeger PE,White DW,Jirousek MR,Trevillyan JM||Molecular and cellular endocrinology (195:109)||2002|
The ribosomal S6 kinases, cAMP-responsive element-binding, and STAT3 proteins are regulated by different leukemia inhibitory factor signaling pathways in mouse embryonic stem cells.
||Boeuf H,Merienne K,Jacquot S,Duval D,Zeniou M,Hauss C,Reinhardt B,Huss-Garcia Y,Dierich A,Frank DA,Hanauer A,Kedinger C||The Journal of biological chemistry (276:46204)||2001|
Activation of signal transducers and activators of transcription 1 and 3 by leukemia inhibitory factor, oncostatin-M, and interferon-gamma in adipocytes.
||Stephens JM,Lumpkin SJ,Fishman JB||The Journal of biological chemistry (273:31408)||1998|
AW109958, 1110034C02Rik, HIES, Aprf, APRF
DNA-binding protein APRF, acute-phase response factor, signal transducer and activator of transcription 3, acute phase response factor, Signal transducer and activator of transcription 3, STAT3, APRF