All Photos(1)
Synonym(s):
APY 29, APY-29, APY29 (type I kinase inhibitor), N2-(1H-Benzo[d]imidazol-6-yl)-N4-(3-cyclopropyl-1H-pyrazol-5-yl)pyrimidine-2,4-diamine, N2-1H-Benzimidazol-6-yl-N4-(5-cyclopropyl-1H-pyrazol-3-yl)-2,4-pyrimidinediamine
Empirical Formula (Hill Notation):
C17H16N8
CAS Number:
Molecular Weight:
332.36
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.77
Recommended Products
Assay
≥97% (HPLC)
form
powder
color
white to beige
solubility
DMSO: 2 mg/mL, clear
storage temp.
−20°C
SMILES string
C1(NC2=CC(C3CC3)=NN2)=CC=NC(NC4=CC=C(N=CN5)C5=C4)=N1
InChI
1S/C17H16N8/c1-2-10(1)13-8-16(25-24-13)22-15-5-6-18-17(23-15)21-11-3-4-12-14(7-11)20-9-19-12/h3-10H,1-2H2,(H,19,20)(H3,18,21,22,23,24,25)
InChI key
WJNBSTLIALIIEW-UHFFFAOYSA-N
General description
APY29 is considered as a type I kinase inhibitor of inositol requiring kinase enzyme 1 α (IRE1α).
Biochem/physiol Actions
APY29 has the ability to enhance inositol requiring kinase enzyme 1 α (IRE1α) (P830L)′s oligomeric state to rescue RNase activity.
APY29 is a small molecule that inhibits the kinase activity of IRE1α (in vitro autophosphorylation IC50 = 280 nM) by targeting its active site ATP-binding pocket, while simultaneously acting as an allosteric activator of IRE1α RNase activity (EC50 = 460 nM) by keeping the active site in an open conformation. When applied 1 hr prior to stress induction by 4-hr 6 nM thapsigargin treatment, APY29 significantly potentiates stress-induced unfolded protein response (UPR) in rat insulinoma INS-1 cultures (XBP1 mRNA processing induction = 54% without vs. 78% with 1-hr 3 μM APY29 pretreatment).
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Alexei V Korennykh et al.
BMC biology, 9, 47-47 (2011-07-07)
The unfolded protein response (UPR) controls the protein folding capacity of the endoplasmic reticulum (ER). Central to this signaling pathway is the ER-resident bifunctional transmembrane kinase/endoribonuclease Ire1. The endoribonuclease (RNase) domain of Ire1 initiates a non-conventional mRNA splicing reaction, leading
Rajarshi Ghosh et al.
Cell, 158(3), 534-548 (2014-07-16)
Depending on endoplasmic reticulum (ER) stress levels, the ER transmembrane multidomain protein IRE1α promotes either adaptation or apoptosis. Unfolded ER proteins cause IRE1α lumenal domain homo-oligomerization, inducing trans autophosphorylation that further drives homo-oligomerization of its cytosolic kinase/endoribonuclease (RNase) domains to
Airong Su et al.
Viruses, 9(9) (2017-08-24)
In response to the endoplasmic reticulum (ER) stress induced by herpes simplex virus type 1 (HSV-1) infection, host cells activate the unfolded protein response (UPR) to reduce the protein-folding burden in the ER. The regulation of UPR upon HSV-1 infection
Alexei V Korennykh et al.
BMC biology, 9, 48-48 (2011-07-07)
Ire1 is a signal transduction protein in the endoplasmic reticulum (ER) membrane that serves to adjust the protein-folding capacity of the ER according to the needs of the cell. Ire1 signals, in a transcriptional program, the unfolded protein response (UPR)
Megan M Robblee et al.
Cell reports, 14(11), 2611-2623 (2016-03-15)
Diets rich in saturated fatty acids (SFAs) produce a form of tissue inflammation driven by "metabolically activated" macrophages. We show that SFAs, when in excess, induce a unique transcriptional signature in both mouse and human macrophages that is enriched by
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