2-Propenoic acid, 3-[7-(β-D-glucopyranosyloxy)-6-benzofuranyl]-, (2Z)-/(2Z)-3-[7-(β-D-Glucopyranosyloxy)-1-benzofuran-6-yl]acrylic acid/Isopsoralenoside
Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
662.4±55.0 °C at 760 mmHg
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provides coniferyl ferulate(CAS#:905954-18-9) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
The endoglycosidase EndoS and the cysteine proteinase SpeB from the human pathogen Streptococcus pyogenes are functionally related in that they both hydrolyze IgG leading to impairment of opsonizing antibodies and thus enhance bacterial survival in human blood. In this study, we further investigated the relationship between EndoS and SpeB by examining their in vitro temporal production and stability and activity of EndoS. Furthermore, theoretical structure modeling of EndoS combined with site-directed mutagenesis and chemical blocking of amino acids was used to identify amino acids required for the IgG glycan-hydrolyzing activity of EndoS.
We could show that during growth in vitro S. pyogenes secretes the IgG glycan-hydrolyzing endoglycosidase EndoS prior to the cysteine proteinase SpeB. Upon maturation SpeB hydrolyzes EndoS that then loses its IgG glycan-hydrolyzing activity. Sequence analysis and structural homology modeling of EndoS provided a basis for further analysis of the prerequisites for IgG glycan-hydrolysis. Site-directed mutagenesis and chemical modification of amino acids revealed that glutamic acid 235 is an essential catalytic residue, and that tryptophan residues, but not the abundant lysine or the single cysteine residues, are important for EndoS activity.
We present novel information about the amino acid requirements for IgG glycan-hydrolyzing activity of the immunomodulating enzyme EndoS. Furthermore, we show that the cysteine proteinase SpeB processes/degrades EndoS and thus emphasize the importance of the SpeB as a degrading/processing enzyme of proteins from the bacterium itself.
EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity
Maria Allhorn,1 Arne Olsen,1,2 and Mattias Collincorresponding author1
An account is given of the twelve species of Leptomias Faust, 1886 occurring in the Sichuan Province of China, including the description of a new species, Leptomias verticalis Ren, Zhang & Song, sp. n. from Jiulong County, Southwest Sichuan. New locality data and remarks for the other eleven species, a key to and distribution map of all twelve Sichuan species are provided. Leptomias chenae Alonso-Zarazaga & Ren is transferred to Geotragus Schoenherr, 1845, where its valid name is G. granulatus (Chao, 1980), comb. n. in application of Art. 59.4. Structural details of Leptomias verticalis and Geotragus granulatus are illustrated.
Distribution, Geotragus, new species, Tanymecini, Weevils
Review of the species of Leptomias Faust from Sichuan, China (Coleoptera, Curculionidae, Entiminae)
Zhenzhen Song,1 Li Ren,2 Runzhi Zhang,2 and Chenggang Zhou1
Targeted anticancer therapies rely on the identification of patient subgroups most likely to respond to treatment. Predictive biomarkers play a key role in patient selection, while diagnostic and prognostic biomarkers expand our understanding of tumor biology, suggest treatment combinations, and facilitate discovery of novel drug targets. We have developed a high-throughput microfluidics method for mutation detection (MUT-MAP, mutation multi-analyte panel) based on TaqMan or allele-specific PCR (AS-PCR) assays. We analyzed a set of 71 mutations across six genes of therapeutic interest. The six-gene mutation panel was designed to detect the most common mutations in the EGFR, KRAS, PIK3CA, NRAS, BRAF, and AKT1 oncogenes. The DNA was preamplified using custom-designed primer sets before the TaqMan/AS-PCR assays were carried out using the Biomark microfluidics system (Fluidigm; South San Francisco, CA). A cross-reactivity analysis enabled the generation of a robust automated mutation-calling algorithm which was then validated in a series of 51 cell lines and 33 FFPE clinical samples. All detected mutations were confirmed by other means. Sample input titrations confirmed the assay sensitivity with as little as 2 ng gDNA, and demonstrated excellent inter- and intra-chip reproducibility. Parallel analysis of 92 clinical trial samples was carried out using 2-100 ng genomic DNA (gDNA), allowing the simultaneous detection of multiple mutations. DNA prepared from both fresh frozen and formalin-fixed, paraffin-embedded (FFPE) samples were used, and the analysis was routinely completed in 2-3 days: traditional assays require 0.5-1 µg high-quality DNA, and take significantly longer to analyze. This assay can detect a wide range of mutations in therapeutically relevant genes from very small amounts of sample DNA. As such, the mutation assay developed is a valuable tool for high-throughput biomarker discovery and validation in personalized medicine and cancer drug development.
Mutation Scanning Using MUT-MAP, a High-Throughput, Microfluidic Chip-Based, Multi-Analyte Panel
Rajesh Patel, 1 , * Alison Tsan, 2 Rachel Tam, 1 Rupal Desai, 1 Nancy Schoenbrunner, 2 Thomas W. Myers, 3 Keith Bauer, 3 Edward Smith, 3 and Rajiv Raja 1