HELLMANEX II PDF

HA_Dosing_table_Hellmanex®III_pdf. Download: Dosing table Hellmanex ® III ( kB). Care should be taken when using ultrasound to clean cells. Material Safety Data Sheet according to Regulation (EC) / Product name: HELLMANEX II. Version: Revision: Hellmanex™ III Special Cleaning Concentrate for cuvettes; find Supelco- Z MSDS, related peer-reviewed papers, technical documents, similar products.

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They are thus hazardous and there is need for decontamination and inactivation procedures for laboratory surfaces hellamnex non-disposable material. We assessed the effectiveness of different reagents to clean and disassemble potentially pathogenic assemblies adsorbed on non-disposable materials in laboratories.

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We provide an integrated representation where desorption and neutralization efficacy and surface compatibility are combined to facilitate the choice of the most adapted decontamination procedure. This representation, together with good laboratory practices, contributes to reducing potential health hazards associated to manipulating protein assemblies with prion-like properties.

Consequently, to minimize the risk associated to exposure of workers in the laboratory to those assemblies it is not only important to develop guidelines for how to best handle those assemblies in the laboratory but also to develop cleaning methods that allow reducing the potential hazard associated to their manipulation. Decontamination and inactivation procedures allowing health hazard reduction by a factor to have been implemented in the prion field for reusable material.

This is certainly due to the fact that protein particles, made of different proteins, have distinct properties. We also evaluated in a quantitative manner the protein assemblies disassembling propensities of those cleaning procedures. We show here that the cleaning procedure efficiency depends not only on the nature of the protein assembly but also on the structural characteristics of distinct assemblies made of one given protein e. Our results strongly suggest that the cleaning procedure needs being adapted to the nature of the contaminated surface.

Assessment of the fate of the distinct assemblies and polymorphs that were detached from contaminated surfaces shows that the most efficient cleaning procedures do not necessarily disassemble the assemblies. Thus, the choice of the most adapted cleaning procedure for one given protein assembly or polymorph should integrate the procedure cleaning efficiency and capacity to dismantle assemblies.

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To better mimic the conditions encountered in laboratories where the surfaces are not necessarily smooth, all surfaces were pre-treated with sandpaper to make the surface rougher, increase the attachment of the material and diminish elimination by gentle wiping. The different fibrillar assemblies adhered to the distinct surfaces and the spots were clearly visible by eye or by fluorescence Fig. Fibrillar assemblies and experimental setup A — C electron micrographs of fibrillar assemblies.

The washing procedure consisted of immersing the contaminated surfaces in washing solutions of different compositions under gentle agitation on an orbital shaker as described in the methods section. The surfaces were washed with MilliQ water, dried and the amount of assemblies that remained after washing Fig. The cleaning solution may disassemble the fibrillar assemblies detached from the surfaces to different extents.

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In the case no disassembly occurs within the cleaning solution, the latter needs to be handled as a biohazard while no such requirement is needed in the case of complete disassembly. Efficiency of different cleaning solutions to remove amyloid fibrillar assemblies from plastic, glass, aluminum and stainless steel surfaces. Fibrillar assemblies made of different proteins were removed by the different cleaning solutions with different efficiencies.

We conclude from these measurements that the cleaning solutions need to be adapted not only to the nature of the fibrillar protein assemblies but also to the fibrillar polymorph and the nature of the contaminated material.

Sodium hydroxide 1N in milliQ water performed well except for plastic and stainless steel surfaces. We conclude from these measurements that the cleaning solutions need to be adapted to the nature of the fibrillar protein assemblies and to the fibrillar polymorphs. As the cleaning solutions need to be adapted to the nature of the fibrillar protein assemblies, the fibrillar polymorphs and to the nature of the contaminated surface, we combined the desorption and neutralization efficacy of each treatment into a unique representation Fig.

Combined representation of the cleaning procedures desorption and neutralization efficacies and compatibility with the contaminated surfaces. This representation combines the desorption and fibrils disassembly efficiency of each experimental treatment and the compatibility of the treatment with the nature of the surfaces.

Colors spanning from brown high to dark green low integrate the proportion of material remaining adsorbed and of fibrillar nature. Hatched boxes indicate that the treatment corrodes the surface. None of the fibrillar assemblies listed and used in this work has been demonstrated to be infectious in humans.

Laboratory Standard Operating Procedures for fibrillar protein assemblies with prion-like properties. The results we report show unequivocally the need to adapt the cleaning procedure to the nature of the fibrillar protein assemblies and the fibrillar polymorphs. Indeed, the cleaning procedure efficiency appears to depend on the nature of the protein assembly and the structural characteristics of distinct assemblies made of one given protein e.

Our results also reveal that the nature of the contaminated surface strongly influences the cleaning procedure efficacy. Our measurements show that the most efficient desorption procedures do not necessarily dismantle distinct assemblies and polymorphs.

Finally, our assessment reveals incompatibilities between certain detergents and surfaces. They thus appear not to be adequate for decontaminating non-disposable laboratory tools made of aluminum. A unique representation Fig. This representation contributes to reducing potential health hazards associated to manipulating protein assemblies with prion-like properties in laboratories. It is worth noting that cleaning was achieved throughout this study by immersing the contaminated surfaces in washing solutions of different compositions under gentle agitation.

Wiping the contaminated surfaces following their exposure to the cleaning solutions with inactivation solution and disposable tissues improves decontamination while generating additional waste. The following reagent were used in this studies: Finally slides and plates were recovered and allowed to dry over night at room temperature in the dark.

The background was measured on a neighboring area and subtracted. The proportion of remaining protein was calculated for each spot as the fluorescence intensity after cleaning divided by the initial fluorescence intensity.

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We acknowledge Patrick Parra for helping us preparing the slides and plates used in the study. Supplementary information accompanies this paper at Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

National Center for Biotechnology InformationU. Published online Jul Author information Article notes Copyright and License information Disclaimer. Received Apr 20; Accepted Jun To view a copy of this license, visit http: Open in a separate window. Cleaning procedure The washing procedure consisted of immersing the contaminated surfaces in washing solutions of different compositions under gentle agitation on an orbital shaker as described in the methods section.

Discussion None of the fibrillar assemblies listed and used in this work has been demonstrated to be infectious in humans. Table 1 Laboratory Standard Operating Procedures for fibrillar protein assemblies with prion-like properties.

Storage – Keep fibrils in closed tubes and discard in biohazard container immediately after use. Methods Reagents used for decontamination The following reagent were used in this studies: Electronic supplementary material Figure S1, Figure S2 1. Notes Competing Interests The authors declare no competing interests. Footnotes Electronic supplementary material Supplementary information accompanies this paper at How the shapes of seeds can influence pathology.

Prion-like transmission of protein aggregates in neurodegenerative diseases. Clavaguera F, et al. Transmission and spreading of tauopathy in transgenic mouse brain. Guo JL, et al. Kaufman SK, et al.

Narasimhan S, et al.

Hellmanex III – Certificate of Analysis

Pathological tau strains from human brains recapitulate the diversity of tauopathies in non-transgenic mouse brain. Sanders DW, et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Carlson GA, et al. Formation, release, and internalization of stable tau oligomers in cells. Woerman AL, et al. Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology.

Desplats P, et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Luk KC, et al. Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Volpicelli-Daley LA, et al.

Exogenous alpha-synuclein fibrils induce Lewy Body pathology leading to synaptic dysfunction and neuron death. Bousset L, et al. Structural and functional characterization of two alpha-synuclein strains. Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice. Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice.

Mougenot AL, et al. Prion-like acceleration of a-synucleinopathy in a transgenic mouse model. Peelaerts W, et al. Recasens A, et al. Lewy body extracts from Parkinson disease brains trigger alpha-synuclein pathology and neurodegeneration in mice and monkeys. Watts JC, et al. Transmission of multiple system atrophy prions to transgenic mice.

Shimozawa A, et al. Propagation of pathological alpha-synuclein in marmoset brain. Eisele YS, et al. Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis.

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