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4-Aminophenylphosphorylcholine Sale

(Synonyms: 4-氨基苯基磷酰胆碱) 目录号 : GC42341

A probe used in affinity precipitation experiments

4-Aminophenylphosphorylcholine Chemical Structure

Cas No.:102185-28-4

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5mg
¥599.00
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10mg
¥1,147.00
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25mg
¥2,399.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

4-Aminophenylphosphorylcholine is a probe that can be conjugated to sepharose in order to generate an adsorbent for use in affinity precipitation experiments.

Chemical Properties

Cas No. 102185-28-4 SDF
别名 4-氨基苯基磷酰胆碱
Canonical SMILES NC1=CC=C(OP(OCC[N+](C)(C)C)([O-])=O)C=C1
分子式 C11H19N2O4P 分子量 274.3
溶解度 PBS (pH 7.2): 10 mg/ml 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 3.6456 mL 18.2282 mL 36.4564 mL
5 mM 0.7291 mL 3.6456 mL 7.2913 mL
10 mM 0.3646 mL 1.8228 mL 3.6456 mL
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Research Update

A new ultralow fouling surface for the analysis of human plasma samples with surface plasmon resonance

Talanta 2021 Jan 1;221:121483.PMID:33076094DOI:10.1016/j.talanta.2020.121483.

Surface plasmon resonance (SPR) has been widely used to detect a variety of biomolecular systems, but only a small fraction of applications report on the analysis of patients' samples. A critical barrier to the full implementation of SPR technology in molecular diagnostics currently exists for its potential application to analyze blood plasma or serum samples. Such capability is mostly hindered by the non-specific adsorption of interfering species present in the biological sample at the functional interface of the biosensor, often referred to as fouling. Suitable polymeric layers having a thickness ranging from 15 and about 70 nm are usually deposited on the active surface of biosensors to introduce antifouling properties. A similar approach is not fully adequate for SPR detection where the exponential decay of the evanescent plasmonic field limits the thickness of the layer beyond the SPR metallic sensor surface for which a sensitive detection can be obtained. Here, a triethylene glycol (PEG(3))-pentrimer carboxybetaine system is proposed to fabricate a new surface coating bearing excellent antifouling properties with a thickness of less than 2 nm, thus compatible with sensitive SPR detection. The high variability of experimental conditions described in the literature for the quantitative assessment of the antifouling performances of surface layers moved us to compare the superior antifouling capacity of the new pentrimeric system with that of 4-Aminophenylphosphorylcholine, PEG-carboxybetaine and sulfobetaine-modified surface layers, respectively, using undiluted and diluted pooled human plasma samples. The use of the new coating for the immunologic SPRI biosensing of human arginase 1 in plasma is also presented.

A novel phosphorylcholine-binding protein from rat serum and its effect on heparin-lipoprotein complex formation in the presence of calcium

J Biol Chem 1981 Jul 25;256(14):7440-6.PMID:6788770doi

An adsorbent was synthesized by attaching 4-Aminophenylphosphorylcholine to cyanogen bromide-activated Sepharose. A phosphorylcholine (P-choline)-binding protein from rat serum was adsorbed on this affinity column which was eluted by 4 mM P-choline. The protein separated into two bands of Mr = 47,000 and 24,000 on sodium dodecyl sulfate-polyacrylamide gradient gels and contained 18% carbohydrate. A serum protein factor, precipitable by 30-50% (NH4)2SO4, was previously shown to inhibit Ca2+-heparin-rat serum very low density lipoprotein (VLDL) precipitation reaction, whereas P-choline counteracted the action of this protein (Mookerjea, S. (1978) Can. J. Biochem. 56, 746-752). It is now demonstrated that purified P-choline-binding protein prevents Ca2+-heparin-chylomicron or VLDL complex formation and P-choline reverses the effect of this protein. Antibody to P-choline-binding protein raised in rabbits produced a single precipitin line against the pure antigen. The antiserum, however, did not react against rat serum chylomicron, VLDL, low density lipoproteins, or high density lipoprotein. Human serum appears to lack P-choline-binding protein, since (a) the affinity column did not adsorb any such protein, (b) P-choline had no effect on the Ca2+-heparin-serum lipoprotein precipitation reaction, and (c) an immunodiffusion test against the antiserum was negative. However, when P-choline-binding protein was added to human serum, the lipoprotein precipitation was inhibited, and P-choline counteracted the effect of this protein. Preliminary experiments suggested a stoichiometric interaction between P-choline-binding protein and VLDL. Hydrophilic P-choline groups exposed on the surface of VLDL may possibly interact with the P-choline-binding protein and thereby affect the precipitation of lipoproteins by heparin and Ca2+.