Anti-phospho-STAT1 (pSer727) antibody produced in rabbit
affinity isolated antibody
別名:
Anti-DKFZp686B04100 antibody produced in rabbit, Anti-ISGF-3 antibody produced in rabbit, Anti-STAT91 antibody produced in rabbit, Anti-signal transducer and activator of transcription 1, 91kDa antibody produced in rabbit
Peptide sequence around phosphorylation site of serine 727 (P-M-S(p)-P-E), according to the protein STAT1.
特徴および利点
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ターゲットの説明
Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. 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.
物理的形状
PBS(0.02% アジ化ナトリウム、50% グリセロール含有)
免責事項
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Journal of cellular physiology, 234(5), 6917-6926 (2018-11-28)
Imbalance of M1/M2 macrophages phenotype activation is a key point in diabetic nephropathy (DN). This study aimed to investigate whether active vitamin D (VD) suppresses macrophage transition to the M1 phenotype via inhibiting the high glucose-induced STAT-1 phosphorylation to reduce