STAT5-IN-1 - CAS 285986-31-4
Catalog number: B0084-007364
Category: Inhibitor
Not Intended for Therapeutic Use. For research use only.
Molecular Formula:
Molecular Weight:
STAT5-IN-1, a cell-permeable nonpeptidic nicotinoyl hydrazone compound, is a selective STAT5 inhibitor with an IC50 of 47 μM for STAT5β isoform with much less effect towards the SH2 domain of STAT1, STAT3, or Lck (IC50>500 µM).
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B0084-007364 50 mg $385 In stock
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Brife Description:
A STAT5 inhibitor
N-[(E)-(4-oxochromen-3-yl)methylideneamino]pyridine-3-carboxamide; STAT5 Inhibitor
DMSO: ≥23.0 mg/mL
Store in a cool and dry place (or refer to the Certificate of Analysis).
Melting Point:
214-216 ℃
1.33±0.1 g/cm3
Canonical SMILES:
1.STAT5 polarization promotes iTregs and suppresses human T-cell alloresponses while preserving CTL capacity.
Betts BC;Veerapathran A;Pidala J;Yu XZ;Anasetti C J Leukoc Biol. 2014 Feb;95(2):205-13. doi: 10.1189/jlb.0313154. Epub 2013 Sep 25.
Alloreactivity negatively influences outcomes of organ transplantation or HCT from allogeneic donors. Standard pharmacologic immune suppression impairs T-cell function and jeopardizes the beneficial reconstitution of Tregs. Murine transplantation models have shown that STAT3 is highly expressed in alloreactive T cells and may be therapeutically targeted. The influence and effects of STAT3 neutralization in human alloreactivity, however, remain to be elucidated. In this study, S3I-201, a selective small-molecule inhibitor of STAT3, suppressed human DC-allosensitized T-cell proliferation and abrogated Th17 responses. STAT3 blockade significantly enhanced the expansion of potent iTregs and permitted CD8(+) cytolytic effector function. Mechanistically, S3I-201 polarized the ratio of STAT phosphorylation in favor of STAT5 over STAT3 and also achieved a significant degree of Foxp3 demethylation among the iTregs. Conversely, selective impairment of STAT5 phosphorylation with CAS 285986-31-4 markedly reduced iTregs. STAT3 represents a relevant target for achieving control over human alloresponses, where its suppression facilitates STAT5-mediated iTreg growth and function.
2.Energy-sensitive regulation of Na+/K+-ATPase by Janus kinase 2.
Bhavsar SK;Hosseinzadeh Z;Brenner D;Honisch S;Jilani K;Liu G;Szteyn K;Sopjani M;Mak TW;Shumilina E;Lang F Am J Physiol Cell Physiol. 2014 Feb 15;306(4):C374-84. doi: 10.1152/ajpcell.00320.2013. Epub 2013 Dec 4.
Janus kinase 2 (JAK2) contributes to intracellular signaling of leptin and erythropoietin, hormones protecting cells during energy depletion. The present study explores whether JAK2 is activated by energy depletion and regulates Na(+)/K(+)-ATPase, the major energy-consuming pump. In Jurkat cells, JAK2 activity was determined by radioactive kinase assay, phosphorylated JAK2 detected by Western blotting, ATP levels measured by luciferase assay, as well as Na(+)/K(+)-ATPase α1-subunit transcript and protein abundance determined by real-time PCR and Western blotting, respectively. Ouabain-sensitive K(+)-induced currents (Ipump) were measured by whole cell patch clamp. Ipump was further determined by dual-electrode voltage clamp in Xenopus oocytes injected with cRNA-encoding JAK2, active (V617F)JAK2, or inactive (K882E)JAK2. As a result, in Jurkat T cells, JAK2 activity significantly increased following energy depletion by sodium azide (NaN3) or 2,4- dinitro phenol (DNP). DNP- and NaN3-induced decrease of cellular ATP was significantly augmented by JAK2 inhibitor AG490 and blunted by Na(+)/K(+)-ATPase inhibitor ouabain. DNP decreased and AG490 enhanced Ipump as well as Na(+)/K(+)-ATPase α1-subunit transcript and protein abundance.
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