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  • Brand : BIOFRON

  • Catalogue Number : BN-O0980

  • Specification : 98%(HPLC)

  • CAS number : 19764-35-3

  • Formula : C15H20O7

  • Molecular Weight : 312.32

  • PUBCHEM ID : 14048613

  • Volume : 5mg

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Catalogue Number


Analysis Method






Molecular Weight




Botanical Source

Structure Type



Standards;Natural Pytochemical;API




p-coumaryl alcohol β-D-glucopyranoside/Triandrin/[3-(4-Hydroxyphenyl)-prop-2-enyl]-β-D-glucopyranosid/Triandrin/<3-(4-Hydroxyphenyl)-prop-2-enyl>-β-D-glucopyranosid/4-hydroxycinnamyl β-D-glucopyranoside





Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.

Flash Point

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InChl Key


WGK Germany


HS Code Reference


Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

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provides coniferyl ferulate(CAS#:19764-35-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

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Protein-protein interactions are essential for the control of cellular functions and are critical for regulation of the immune system. One example is the binding of Fc regions of IgG to the Fc gamma receptors (FcγRs). High sequence identity (98%) between the genes encoding FcγRIIIa (expressed on macrophages and natural killer cells) and FcγRIIIb (expressed on neutrophils) has prevented the development of monospecific agents against these therapeutic targets. We now report the identification of FcγRIIIa-specific artificial binding proteins called “Affimer” that block IgG binding and abrogate FcγRIIIa-mediated downstream effector functions in macrophages, namely TNF release and phagocytosis. Cocrystal structures and molecular dynamics simulations have revealed the structural basis of this specificity for two Affimer proteins: One binds directly to the Fc binding site, whereas the other acts allosterically.


Fc gamma receptor IIIa, specific inhibitor, Affimer, allosteric, competitive


Affimer proteins inhibit immune complex binding to FcγRIIIa with high specificity through competitive and allosteric modes of action


James I. Robinson,a,b Euan W. Baxter,a,b,1 Robin L. Owen,c,1 Maren Thomsen,d,1 Darren C. Tomlinson,d,e,1 Mark P. Waterhouse,a,b,1 Stephanie J. Win,a,b Joanne E. Nettleship,f,g Christian Tiede,e Richard J. Foster,d,h Raymond J. Owens,f,g Colin W. G. Fishwick,d,h Sarah A. Harris,d,i Adrian Goldman,e,j Michael J. McPherson,d,e,2 and Ann W. Morgana,b,2

Publish date

2018 Jan 2;




Understanding molecular interactions on immune cells is crucial for drug development to treat cancer and autoimmune diseases. When characterizing molecular interactions, the use of a relevant living model system is important, as processes such as receptor oligomerization and clustering can influence binding patterns. We developed a protocol to enable time-resolved analysis of ligand binding to receptors on living suspension cells. Different suspension cell lines and weakly adhering cells were tethered to Petri dishes with the help of a biomolecular anchor molecule, and antibody binding was analyzed using LigandTracer. The protocol and assay described in this report were used to characterize interactions involving eight cell lines. Experiments were successfully conducted in three different laboratories, demonstrating the robustness of the protocol. For various antibodies, affinities and kinetic rate constants were obtained for binding to CD20 on both Daudi and Ramos B-cells, the T-cell co-receptor CD3 on Jurkat cells, and the Fcγ receptor CD32 on transfected HEK293 cells, respectively. Analyzing the binding of Rituximab to B-cells resulted in an affinity of 0.7-0.9 nM, which is similar to values reported previously for living B-cells. However, we observed a heterogeneous behavior for Rituximab interacting with B-cells, which to our knowledge has not been described previously. The understanding of complex interactions will be facilitated with the possibility to characterize binding processes in real-time on living immune cells. This provides the chance to broaden the understanding of how binding kinetics relate to biological function.


affinity, kinetics, therapeutic antibody, B-cells, T-cells, CD20, Fcγ receptor


Real-time Characterization of Antibody Binding to Receptors on Living Immune Cells


Sina Bondza,1,2,* Eleanor Foy,3 Jonathan Brooks,4 Karl Andersson,1,2 James Robinson,3 Pascale Richalet,5 and Jos Buijs1,2

Publish date





This study aimed to investigate the methods, effects, and application value of a combination of CO2 laser-assisted uvulopalatopharyngoplasty (UPPP) and selective nasal cavity expansion for the treatment of multiplanar narrowing-induced obstructive sleep apnea hypopnea syndrome (OSAHS). Ninety-three patients with OSAHS and multiplanar stenosis were treated with CO2 laser-assisted modified UPPP and selective surgical expansion of the nasal cavity, with 12 completing the operation in stages. Six months after the operation, 23 patients (24.7%) were effectively cured, 52 (55.9%) had excellent efficacy, and 18 (19.4%) were cured, and the total efficacy was 100%. One year after the surgery, the surgical outcomes of 65 patients were reviewed, and the surgeries were ineffective in four (6.2%), effective in 14 (21.5%), very effective in 36 (55.4%), and curative in 11 (16.9%), and the total efficacy was 93.8%. Another 93 cases were treated with the traditional UPPP method only. At the six-month postoperative review, 18 (19.4%) were effectively cured, 30 (32.3%) had excellent efficacy, and 10 (10.8%) were cured, while the surgery was ineffective in 35 (37.6%). The total efficacy was 62.4%. One year after the surgery, the surgical outcomes of 75 patients were reviewed, and the surgeries were ineffective in 29 (38.7%), effective in 14 (18.7%), very effective in 24 (32.0%), and curative in eight (10.7%), and the total efficacy was 61.3%. Compared to the traditional operative methods, the treatment with one operation involving CO2-laser-assisted UPPP and selective nasal cavity expansion was thoroughly effective on multiple stenosis sites, including nasal, nasopharyngeal, and oropharyngeal airways. However, potential complications must be carefully avoided.


Obstructive sleep apnea hypopnea syndrome, modified uvulopalatopharyngoplasty, selective expansion of the nasal cavity


Combination of CO2 laser-assisted uvulopalatopharyngoplasty and nasal cavity expansion enhances treatment of obstructive sleep apnea-hypopnea syndrome


De Huai, Jun Dai, Min Xu, Ying Cao, Hongmao Song, Shoufeng Wang, Haixu Wang, Min Yin, Lei Cheng, Yalong Zhang, Xiaojian Zhou, Jianwu Wang

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