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Because ATP and ATP analogs partially displace complexed bis-ANS it has also been possible to study interactions of S-1 and nucleotides by using the displacement effect. Approximate values of the parameters of these various interactions have been measured. Some possible applications of bis-ANS have been explored.
Titration of bisANS binding. Binding of bisANS to G protein (A and B
compound Summary 4,4'-Dianilino-1,1'-binaphthyl-5,5'-disulfonic acid dipotassium salt PubChem CID 16213473 Structure Chemical Safety Laboratory Chemical Safety Summary (LCSS) Datasheet Molecular Formula C32H22K2N2O6S2 Synonyms Bis-ans 65664-81-5 4,4'-Dianilino-1,1'-binaphthyl-5,5'-disulfonic acid dipotassium salt Bis-ANS (dipotassium)
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Bis-ANS was the most effective inhibitor of prion peptide aggregation. Bis-ANS binds strongly to rPrP 23-231 leading to a substantial increase in -sheet content and to limited oligomerization.
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Despite emergence of bis-ANS as a major fluorescence probe of proteins structure, conformational and spectroscopic properties of protein/bis-ANS complexes remains largely unexplored. We have shown that fluorescence polarization of both ANS and bis-ANS is excitation wavelength dependent and this is a property of all protein-ANS/bis-ANS complexes.
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Bis-ANS exhibits a chaperone-like activity, effectively suppressing protein aggregation and preventing a certain degree of heat-inactivation of enzymes [5]. Horowitz et al. have recently shown that bis-ANS binds to tubulin, inhibiting the formation of microtubules [2], [11]. Their experiments demonstrate the presence of more than one site for.
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Product Overview Documents Bis-ANS is superior to 1-8-ANS as a probe for nonpolar cavities in proteins, often binding with an affinity that is orders-of-magnitude higher. Anilinonaphthalene sulfonates (ANS) are essentially nonfluorescent in water, only becoming appreciably fluorescent when bound to membranes.
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open access Highlights • Fluorescence-based assay is a fast and easy tool for detection of RNA-IFIT binding. • Bis-ANS probe demonstrates effective binding to the IFIT proteins. • Bis-ANS is located inside the RNA binding tunnel of the IFIT proteins. • Developed assay enables binding studies at low RNA concentrations. Abstract Keywords IFIT
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Bis-ANS is a fluorescent probe for nonpolar cavities in proteins. Used to detect A β fibre (K d = ~80 nM); exhibits distinct fluorescent profiles for fibres and oligomers. Fluoresces in hydrophobic environments, negligible fluorescence in water solutions. Excitation\emission λ ~ 355\520 nm at pH 7.4. Also modulates liquid-liquid phase.
BisANS induces LLPS of the TDP43 LCD a Chemical structure of
5,5'-Bis [8- (phenylamino)-1-naphthalenesulfonate] (bis-ANS), the fluorescent probe which binds to tubulin, inhibits its assembly into microtubules [Horowitz et al. (1984) J. Biol. Chem. 259, 14647-14650].
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9619517 DOI: 10.1080/07391102.1998.10508216 Abstract Despite emergence of bis-ANS as a major fluorescence probe of proteins structure, conformational and spectroscopic properties of protein/bis-ANS complexes remains largely unexplored.
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Bis-ANS is superior to 1-8-ANS as a probe for nonpolar cavities in proteins, often binding with an affinity that is orders-of-magnitude higher. Anilinonaphthalene sulfonates Invitrogen Bis-ANS (4,4'-Dianilino-1,1'-Binaphthyl-5,5'-Disulfonic Acid, | Fisher Scientific
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Background and objective: Published algorithms for classification of human sperm heads are based on relatively small image databases that are not open to the public, and thus no direct comparison is available for competing methods. We describe a gold-standard for morphological sperm analysis (SCIAN-MorphoSpermGS), a dataset of sperm head images with expert-classification labels in one of the.
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ANS has the potential to characterize proteins in solid states. • ANS fluorescence in protein films reveals the hydrophobic sites with distinct properties. • Short lifetime DAS of ANS in hydrated protein films is similar to that of ANS-protein complexes in solution. •
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bis-ANS 1,1′-bi (4-anilino)naphtalene-5,5′-disulfonic acid α-Crystallin, a major lens protein, plays an important role in maintaining the transparency and refractive properties of the eye lens ( 1., 2., 3. ). The lenticular α-crystallin consists of two 20-kDa polypeptide chains, αA and αB, that share about 60% sequence homology.
(A) Change of bisANS fluorescence intensity (fluorescence maximum, λ
Depending on context, bis-ANS can both induce LLPS de novo as well as prevent formation of homotypic liquid droplets. Our study also reveals the mechanisms by which bis-ANS and related.
Threedimensional structure of bisANS. For clarity only polar
These results resemble effects of bis-ANS on BSA, where low ratios of bis-ANS:protein were found to increase thermostability of BSA, while higher ratios induced transition of the protein into a molten globule-like state (Celej et al. 2003). Therefore, we propose that accelerated aggregation of IL-1ra in the presence of 4.2-21 mM ANS reflects.