White needle crystal
Pinus cembra L./Alpinia oxyphylla Miq.
Methyl chrysin/5-hydroxy-7-methoxy-flavone/5-Hydroxy-7-methoxy-2-phenyl-4H-chromen-4-one/5-OH-7-methoxyflavone/7-methoxycrysin/Tectochrysin/4H-1-Benzopyran-4-one, 5-hydroxy-7-methoxy-2-phenyl-/5-hydroxy-7-methoxy-2-phenylchromen-4-one/Flavone,5-hydroxy-7-methoxy/7-Methoxy-5-hydroxyflavone/4H-1-Benzopyran-4-one,5-hydroxy-7-methoxy-2-phenyl/5-HYDROXY-7-METHOXYFLAVONE/Flavone, 5-hydroxy-7-methoxy-/7-O-methylchrysin/Techtochrysin
Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
487.4±45.0 °C at 760 mmHg
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:520-28-5) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Background & aim
Due to known limitations of liver biopsy, reliable non-invasive serum biomarkers for chronic liver diseases are needed. We performed serum peptidomics for such investigation in compensated chronic hepatitis B (CHB) patients.
Liquid chromatography combined with tandem mass spectrometry (LC-MS/MS) was used to identify differentially expressed peptides in sera from 40 CHB patients (20 with S0G0-S1G1 and 20 with S3G3-S4G4). Ion pair quantification from differentially expressed peptides in a validation set of sera from 86 CHB patients was done with multiple reaction monitoring (MRM).
21 differentially represented peptide peaks were found through LC-MS/MS. Ion pairs generated from eleven of these peptides (m/z < 800) were quantified by MRM. Summed peak area ratios of 6 ion pairs from peptide m/z 520.3 (176.1, 353.7, 459.8, 503.3, 351.3, 593.1), which was identified as dihydroxyacetone kinase (DAK) fragment, decreased from mild to advanced stages of fibrosis or inflammation. Area Under Receiver Operating Characteristic Curves (AUROCs) of five ion models discriminating fibrosis degrees were 0.871 ~ 0.915 (S2-4 versus S0-1) and 0.804 ~ 0.924 (S3-4 versus S0-2). AUROCs discriminating inflammation grades were 0.840 ~ 0.902 (G2-4 versus G0-1) and 0.787 ~ 0.888 (G3-4 versus G0-2). The diagnostic power of these models provides improved sensitivity and specificity for predicting disease progression as compared to aspartate aminotransferase to platelet ratio index (APRI), FIB-4, Forn’s index and serum DAK protein. Conclusions The peptide fragment (m/z 520.3) of DAK is a promising biomarker to guide timing of antiviral treatment and to avoid liver biopsy in compensated CHB patients.
Peptidome, Dihydroxyacetone kinase, Chronic hepatitis B, Multiple reaction monitoring, Liquid chromatography combined with tandem mass spectrometry
Serum dihydroxyacetone kinase peptide m/z 520.3 as predictor of disease severity in patients with compensated chronic hepatitis B
Ming-Yi Xu,#1 Xiao-Fang Jia,#2 Ying Qu,1 Rui-Dan Zheng,3 Zheng-Hong Yuan,2 Hong-Lei Weng,4 Steven Dooley,4 Xing-Peng Wang,1 Li-Jun Zhang,corresponding author2 and Lun-Gen Lucorresponding author1
Ebolaviruses cause severe disease in humans, and identification of monoclonal antibodies (mAbs) that are effective against multiple ebolaviruses are important for therapeutics development. Here we describe a distinct class of broadly neutralizing human mAbs with protective capacity against three ebolaviruses infectious for humans: Ebola (EBOV), Sudan (SUDV), and Bundibugyo (BDBV) viruses. We isolated mAbs from human survivors of ebolavirus disease and identified a potent mAb, EBOV-520, which bound to an epitope in the glycoprotein (GP) base region. EBOV-520 efficiently neutralized EBOV, BDBV, and SUDV and also showed protective capacity in relevant animal models of these infections. EBOV-520 mediated protection principally by direct virus neutralization and exhibited multifunctional properties. This study identified a potent naturally occurring mAb and defined key features of the human antibody response that may contribute to broad protection. This multifunctional mAb and related clones are promising candidates for development as broadly protective pan-ebolavirus therapeutic molecules.
ebolavirus, monoclonal antibodies, viral antibodies, neutralizing antibodies, cross protection, heterologous immunity, glycoproteins, Ebola hemorrhagic fever, epitopes, epitope mapping
Multifunctional Pan-ebolavirus Antibody Recognizes a Site of Broad Vulnerability on the Ebolavirus Glycoprotein
Pavlo Gilchuk,1 Natalia Kuzmina,6,7 Philipp A. Ilinykh,6,7 Kai Huang,6,7 Bronwyn M. Gunn,9 Aubrey Bryan,10 Edgar Davidson,10 Benjamin J. Doranz,10 Hannah L. Turner,11 Marnie L. Fusco,13 Matthew S. Bramble,14,15 Nicole A. Hoff,14 Elad Binshtein,4 Nurgun Kose,1 Andrew I. Flyak,2 Robin Flinko,16 Chiara Orlandi,16 Robert Carnahan,1 Erica H. Parrish,1 Alexander M. Sevy,3 Robin G. Bombardi,1 Prashant K. Singh,4 Patrick Mukadi,17 Jean Jacques Muyembe-Tamfum,17 Melanie D. Ohi,4,18 Erica Ollmann Saphire,11,12,13 George K. Lewis,16 Galit Alter,9 Andrew B. Ward,11 Anne W. Rimoin,14 Alexander Bukreyev,6,7,8,18,∗ and James E. Crowe, Jr.1,2,3,5,18,19,∗∗
2018 Aug 21;
ESICM LIVES 2016: part three Milan, Italy. 1-5 October 2016
2016 Sep 29