15803-59-5

Basic information

• Product Name: 1,4-Cyclohexanediamine, N-methyl-, trans-
• Synonyms: S14-2617;trans-N-methylcyclohexane-1,4-diamine;trans-4-(methylamino)cyclohexylamine;1,4-Cyclohexanediamine,N-methyl-,trans
• CAS NO: 15803-59-5
• Molecular Formula: C7H16N2
• Molecular Weight: 128.217
• Mol File: 15803-59-5.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 183.8±8.0 °C(Predicted)
• Density: 0.92±0.1 g/cm3(Predicted)
• CAS DataBase Reference: 1,4-Cyclohexanediamine, N-methyl-, trans-(CAS DataBase Reference)
• NIST Chemistry Reference: 1,4-Cyclohexanediamine, N-methyl-, trans-(15803-59-5)
• EPA Substance Registry System: 1,4-Cyclohexanediamine, N-methyl-, trans-(15803-59-5)

Safety Data

• Hazardous Substances Data: 15803-59-5(Hazardous Substances Data)

Upstream product

• 2615-25-0 trans-1,4-cyclohexyldiamine 
• 177906-48-8 trans-N-Boc-1,4-cyclohexanediamine 
• 566172-78-9 n-butyl trans-(4-aminocyclohexyl)-carbamate 

Downstream Products

• 566172-79-0 trans-N-methyl-N-tert-butoxycarbonyl-1,4-diaminocyclohexane 
• 1025061-41-9 trans-3-{[4-(Boc-methyl-amino)-cyclohexylamino]-methyl}-4-fluoro-benzeneboronic acid 
• 945996-91-8 trans-3-{[4-(Boc-methyl-amino)-cyclohexylamino]-methyl}-4-methoxy-benzeneboronic acid 
• 945998-86-7 trans-tert-butyl {4-[2-methoxy-5-(2-methyl-pyridin-4-yl)-benzylamino]-cyclohexyl}-methyl-carbamate 
• 945997-05-7 trans-3-{[4-(Boc-methyl-amino)-cyclohexylamino]-methyl}-4-ethoxy-benzeneboronic acid 
• 1025060-99-4 trans-tert-butyl {4-[(4'-cyano-4-methoxy-biphenyl-3-ylmethyl)-amino]-cyclohexyl}-methyl-carbamate 
• 945999-95-1 trans-tert-butyl {4-[5-(6-amino-pyridin-3-yl)-2-methoxy-benzylamino]-cyclohexyl}-methyl-carbamate 
• 945997-80-8 trans-tert-butyl {4-[(4'-cyano-4-ethoxy-biphenyl-3-ylmethyl)-amino]-cyclohexyl}-methyl-carbamate 
• 945996-93-0 trans-3-{[[4-(Boc-methyl-amino)-cyclohexyl]-(3-chlorobenzo[b]thiophene-2-carbonyl)-amino]-methyl}-4-methoxy-benzeneboronic acid 
• 945997-08-0 trans-3-{[(4-(Boc-methyl-amino)-cyclohexyl)-(3-chloro-benzo[b]thiophene-2-carbonyl)-amino]-methyl}-4-ethoxy-benzeneboronic acid 
• 945996-95-2 trans-3-{[[4-(Boc-methyl-amino)-cyclohexyl]-(3-chloro-4-fluoro-benzo[b]thiophene-2-carbonyl)-amino]-methyl}-4-methoxy-benzeneboronic acid 
• 1025061-58-8 C₃₅H₄₂ClN₅O₄S 
• 945997-14-8 trans-tert-butyl {4-[(3-chloro-benzo[b]thiophene-2-carbonyl)-(4'-cyano-4-methoxy-biphenyl-5-ylmethyl)-amino]-cyclohexyl}-methyl-carbamate 
• 946000-02-8 trans-methyl 4-(3-{[(3-chloro-4,7-difluoro-benzo[b]thiophene-2-carbonyl)-(4-methylamino-cyclohexyl)-amino]-methyl}-4-methoxy-phenyl)-pyridine-2-carboxylate 

Relevant articles and documents

IRAK DEGRADERS AND USES THEREOF

The present invention provides compounds, compositions thereof, and methods of using the same.

Smooth receptor ligand

The invention relates to the technical field of biology, particularly to a smooth receptor ligand, and provides a smooth receptor ligand or an isomer prodrug, a solvate and a pharmaceutically acceptable salt thereof, wherein the structural formula of the smooth receptor ligand is A-linker-B, A is an extracellular domain ligand structure, B is a transmembrane domain ligand structure, and Linker isa linear subunit inactive to the smooth receptor. According to the novel double-end small molecule ligand for the smooth receptor, by combining the crystal structure data of the smooth receptor, a linker is introduced into the proper sites of an extracellular domain ligand and a transmembrane domain ligand to obtain brand-new double-end ligand small molecules, so that the interaction between the ligand and the receptor and the biological activity of the ligand are enhanced.

Binding to an Unusual Inactive Kinase Conformation by Highly Selective Inhibitors of Inositol-Requiring Enzyme 1α Kinase-Endoribonuclease

A series of imidazo[1,2-b]pyridazin-8-amine kinase inhibitors were discovered to allosterically inhibit the endoribonuclease function of the dual kinase-endoribonuclease inositol-requiring enzyme 1α (IRE1α), a key component of the unfolded protein response in mammalian cells and a potential drug target in multiple human diseases. Inhibitor optimization gave compounds with high kinome selectivity that prevented endoplasmic reticulum stress-induced IRE1α oligomerization and phosphorylation, and inhibited endoribonuclease activity in human cells. X-ray crystallography showed the inhibitors to bind to a previously unreported and unusually disordered conformation of the IRE1α kinase domain that would be incompatible with back-to-back dimerization of the IRE1α protein and activation of the endoribonuclease function. These findings increase the repertoire of known IRE1α protein conformations and can guide the discovery of highly selective ligands for the IRE1α kinase site that allosterically inhibit the endoribonuclease.