This product is isolated and purified from the herbs of Oryza sativa
1,2,3,4,5,6-Cyclohexanehexol, hexakis(dihydrogen phosphate), sodium salt, (1α,2α,3α,4α,5α,6β)- (1:12)/Inositol hexaphosphoric acid/Dodecasodium (1R,2R,3r,4S,5S,6s)-1,2,3,4,5,6-cyclohexanehexayl hexakis(phosphate)/Sodium phytate/myo-Inositol hexakis(dihydrogen phosphate)/Inositol hexakisphosphate
Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
1190.7ºC at 760mmHg
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:14306-25-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
The transcriptional corepressor complex CoREST is one of seven histone deacetylase complexes that regulate the genome through controlling chromatin acetylation. The CoREST complex is unique in containing both histone demethylase and deacetylase enzymes, LSD1 and HDAC1, held together by the RCOR1 scaffold protein. To date, it has been assumed that the enzymes function independently within the complex. Now, we report the assembly of the ternary complex. Using both structural and functional studies, we show that the activity of the two enzymes is closely coupled and that the complex can exist in at least two distinct states with different kinetics. Electron microscopy of the complex reveals a bi-lobed structure with LSD1 and HDAC1 enzymes at opposite ends of the complex. The structure of CoREST in complex with a nucleosome reveals a mode of chromatin engagement that contrasts with previous models.
CoREST complex, RCOR1, HDAC1, LSD1, KDM1A, nucleosome, histone deacetylase, lysine demethylase
Mechanism of Crosstalk between the LSD1 Demethylase and HDAC1 Deacetylase in the CoREST Complex
Yun Song,1,6 Lisbeth Dagil,2,7 Louise Fairall,1 Naomi Robertson,3,8 Mingxuan Wu,4,10 T.J. Ragan,1 Christos G. Savva,1 Almutasem Saleh,1,11 Nobuhiro Morone,5 Micha B.A. Kunze,2,7 Andrew G. Jamieson,3,9 Philip A. Cole,4 D. Flemming Hansen,2,∗ and John W.R. Schwabe1,12,∗∗
2020 Feb 25
Clathrin-mediated endocytosis (CME) is key to maintaining the transmembrane protein composition of cells’ limiting membranes. During mammalian CME, a reversible phosphorylation event occurs on Thr156 of the μ2 subunit of the main endocytic clathrin adaptor, AP2. We show that this phosphorylation event starts during clathrin-coated pit (CCP) initiation and increases throughout CCP lifetime. μ2Thr156 phosphorylation favors a new, cargo-bound conformation of AP2 and simultaneously creates a binding platform for the endocytic NECAP proteins but without significantly altering AP2’s cargo affinity in vitro. We describe the structural bases of both. NECAP arrival at CCPs parallels that of clathrin and increases with μ2Thr156 phosphorylation. In turn, NECAP recruits drivers of late stages of CCP formation, including SNX9, via a site distinct from where NECAP binds AP2. Disruption of the different modules of this phosphorylation-based temporal regulatory system results in CCP maturation being delayed and/or stalled, hence impairing global rates of CME.
clathrin-mediated endocytosis, regulation by phosphorylation, AP2 endocytic adaptor, NECAP, SNX9, AAK1, Numb-associated kinases (NAK), NMR, crystallography, TIRF
Temporal Ordering in Endocytic Clathrin-Coated Vesicle Formation via AP2 Phosphorylation
Antoni G. Wrobel,1,8,9 Zuzana Kadlecova,1,8,10,∗ Jan Kamenicky,2 Ji-Chun Yang,3 Torsten Herrmann,4 Bernard T. Kelly,1 Airlie J. McCoy,1 Philip R. Evans,3 Stephen Martin,5 Stefan Muller,6 Filip Sroubek,2 David Neuhaus,3 Stefan Honing,7,∗∗ and David J. Owen1
2019 Aug 19