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ИНСТРУКЦИЯ № 31/09 по применению щелочного моющего средства «СФЕРА ИНСТРУФОРТЕ» для очистки маникюрного и парикмахерского инструмента

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ИНСТРУКЦИЯ № 31/09

по применению щелочного моющего средства

«СФЕРА ИНСТРУФОРТЕ»

 для очистки маникюрного и парикмахерского инструмента

 

1. ОБЩИЕ СВЕДЕНИЯ

1.1.   Средство «СФЕРА ИНСТРУФОРТЕ» предназначено для очистки маникюрного и парикмахерского инструмента, изготовленного из всех видов материалов, за исключением  алюминия, лёгких и цветных металлов, а также из лужёных и оцинкованных материалов.

1.2    Моющее средство «СФЕРА ИНСТРУФОРТЕ» представляет собой  высоко-концентрированную прозрачную жидкость от светло-жёлтого до тёмно-коричневого цвета, хорошо растворяющуюся в воде, обладающую пониженным пенообразованием. Действующими веществами препарата являются оптимизированная смесь щелочных агентов в комплексе с неионогенным ПАВ, комплексообразователем и ингибитором коррозии. Рабочие растворы препарата имеют значение рН 12,6 ± 0,5 ед.

1.3    Моющее средство «СФЕРА ИНСТРУФОРТЕ» биоразлагаемое, не горючее и не взрывоопасное, в химическом отношении стабильно в воде и на воздухе, не разлагается с выделением вредных веществ. Не содержит фосфатов, агрессивных токсических веществ, растворителей. Не обладает аллергическими и кумулятивными свойствами.

Гарантийный срок хранения средства – 24 месяца со дня изготовления. Рабочие растворы средства «СФЕРА ИНСТРУФОРТЕ» стабильны в течение недели и при хранении не разлагаются. Средство «СФЕРА ИНСТРУФОРТЕ» замерзает при температуре минус 26°С, после размораживания сохраняет свои свойства.

1.4.   Наличие в составе «СФЕРА ИНСТРУФОРТЕ» комплексообразователя позволяет использовать растворы препарата в районах с повышенной жёсткостью воды.

1.5.   Моющее средство «СФЕРА ИНСТРУФОРТЕ» расфасовывают в полиэтиленовые канистры вместимостью 1 л.

1.6.   Средство «СФЕРА ИНСТРУФОРТЕ» по параметрам острой токсичности в соответствии с ГОСТ 12.1.007-76 относится 3 классу опасности (вещества умеренно опасные). Опасно при попадании в глаза, на кожу и при проглатывании. Раздражает (прижигающее действие) кожу, слизистые оболочки глаз (при попадании в глаза химический ожог). В виде паров средство малоопасно согласно классификации ингаляционной опасности средств по степени летучести. Средство не оказывает кумулирующего и сенсибилизирующего действия. Продукт не токсичен при использовании по назначению и правильном обращении. Рабочие растворы могут вызывают сухость и шелушение кожи при многократных повторных аппликациях.

Требования безопасной работы со средством изложены в п. 4 настоящей инструкции.

1.7.   Средство «СФЕРА ИНСТРУФОРТЕ» применимо для мойки инструмента, изготовленного из любого материала, стойкого к щелочам, оно не портит хромоникелевую, нержавеющую сталь, эмалевые покрытия и пластмассы.

1.8.   При работе со средством «СФЕРА ИНСТРУФОРТЕ» не допускается его смешивание с другими химическими веществами, особенно с кислотами.

1.9.   Хранение средства «СФЕРА ИНСТРУФОРТЕ» осуществляют в герметично закрытой таре предприятия-изготовителя в сухом проветриваемом помещении.

2. ПРИГОТОВЛЕНИЕ РАБОЧИХ РАСТВОРОВ

2.1.   Ёмкости для приготовления рабочих растворов должны быть изготовлены из коррозионностойкого материала, и закрываться герметичными крышками.

2.2.   Перед приготовлением рабочих растворов содержимое канистры необходимо аккуратно перемешать.

2.3.   Для приготовления рабочих растворов «СФЕРА ИНСТРУФОРТЕ», а также ополаскивания необходимо использовать водопроводную воду, соответствующую требованиям СанПиН 2.1.4.1074-01.

2.4.   Для очистки инструмента используют средство «СФЕРА ИНСТРУФОРТЕ» в виде водных растворов, концентрация которых установлена в пределах 20 – 50% (по препарату) в зависимости от степени загрязнения. Для приготовления рабочих растворов «СФЕРА ИНСТРУФОРТЕ» в ёмкости заливают воду и растворяют в ней препарат в количестве, необходимом для получения требуемой концентрации.

При приготовлении рабочих растворов средства руководствуются расчётами, приведёнными в таблице 1.

Таблица 1.

Приготовление рабочих растворов моющего средства «СФЕРА ИНСТРУФОРТЕ»

Требуемая концентрация рабочего раствора «СФЕРА ИНСТРУФОРТЕ», % (об.) по средству	Количество средства и воды в расчете на 1 л рабочего раствора
	Количество средства, мл	Количество воды, мл
20	200	800
30	300	700
50	500	500

Примечание: для наиболее рационального расходования моющего средства конкретная концентрация, время выдержки и температура рабочего раствора подбирается экспериментально потребителем в зависимости от характера загрязнений, типа обрабатываемой поверхности и ограничений по времени мойки.

3. УСЛОВИЯ ПРИМЕНЕНИЯ

3.1.   Допускается снижение концентрации, температуры и времени действия препарата в случае использования механической мойки или при незначительных загрязнениях обрабатываемых поверхностей.

3.2.   Время обработки при помощи средства «СФЕРА ИНСТРУФОРТЕ» может быть увеличено при удалении застарелых и трудно поддающихся мойке загрязнений .

3.3.   Оптимальная температура мойки средством «СФЕРА ИНСТРУФОРТЕ» составляет +50…+55°С. Диапазон рабочих температур от +20 до +80°С. При использовании рабочих растворов с температурой ниже +30°С, необходимо увеличить концентрацию моющего средства и/или увеличить время обработки. Использование ершей и щёток при механической очистке сокращает время очистки в 1,5 – 3 раза.

3.4. Для ускорения и оптимизации процесса очистки инструмента рекомендуется использовать средство «СФЕРА ИНСТРУФОРТЕ» с применением УЗО мойки.

3.5. По окончанию очистки инструмент промывается под струей чистой водопроводной воды при температуре +40…+50°С до полного удаления остатков средства.

4. ТРЕБОВАНИЯ К ТЕХНИКЕ БЕЗОПАСНОСТИ

4.1.   При работе со средством «СФЕРА ИНСТРУФОРТЕ» необходимо избегать его попадания на кожу и в глаза.

4.2.   Все работы со средством «СФЕРА ИНСТРУФОРТЕ» следует проводить в защитных резиновых перчатках.

4.3.   Средство «СФЕРА ИНСТРУФОРТЕ» пожаро- взрывобезопасно.

4.4.   При работе со средством следует соблюдать правила личной гигиены. Запрещается курить, пить, принимать пищу.

5. МЕРЫ ПЕРВОЙ ПОМОЩИ ПРИ СЛУЧАЙНОМ ОТРАВЛЕНИИ

5.1.   При попадании концентрата средства «СФЕРА ИНСТРУФОРТЕ» на кожу необходимо смыть его большим количеством воды.

5.2.   При попадании средства в глаза немедленно промыть их под проточной водой в течение 10 – 15 минут. При раздражении слизистых оболочек закапать в глаза 30%-ный раствор сульфацила натрия. При необходимости обратиться к врачу.

5.3.   При попадании средства в желудок выпить несколько стаканов воды с 10 – 20 измельченными таблетками активированного угля (адсорбента). Рвоту не вызывать! При необходимости обратиться к врачу.

Сфера вечного — Path of Exile Wiki

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Сфера вечного — это валюта, которая создает слепок предмета. СлепокВосстанавливает оригинальный предмет по его слепкуЩелкните правой кнопкой мыши по этому объекту, а затем левой по слепку предмета, чтобы восстановить его свойства. Слепок нельзя выбросить или использовать в торговле с другими игроками. может быть использован для возврата предмета в прежнее состояние после того, как на нём были использованы другие виды валют. Этот предмет больше не выпадает в игре, и может быть найден только при торговле на постоянных лигах. However, it can be found as a Relic in the

90000 Overview of Affinity Purification | Thermo Fisher Scientific 90001 90002 Various methods are used to enrich or purify a protein of interest from other proteins and components in a crude cell lysate or other sample. The most powerful of these methods is affinity chromatography, also called affinity purification, whereby the protein of interest is purified by virtue of its specific binding properties to an immobilized ligand.90003 90004 90005 Introduction 90006 90002 Proteins and other macromolecules of interest can be purified from crude extracts or other complex mixtures by a variety of methods.Selective precipitation is perhaps the simplest method for separating one type of macromolecule from another. 90003 90002 Most purification methods, however, involve some form of chromatography whereby molecules in solution (mobile phase) are separated based on differences in chemical or physical interaction with a stationary material (solid phase). Gel filtration (also called size-exclusion chromatography or SEC) uses a porous resin material to separate molecules based on size (i.e., physical exclusion).In ion exchange chromatography, molecules are separated according to the strength of their overall ionic interaction with a solid phase material (i.e., nonspecific interactions). 90003 90002 By contrast, 90012 affinity chromatography 90013 (also called affinity purification) makes use of specific binding interactions between molecules. A particular ligand is chemically immobilized or «coupled» to a solid support so that when a complex mixture is passed over the column, those molecules having specific binding affinity to the ligand become bound.After other sample components are washed away, the bound molecule is stripped from the support, resulting in its purification from the original sample. 90003 90002 Each specific affinity system requires its own set of conditions and presents its own peculiar challenges for a given research purpose. Other Protein Methods articles describe the factors and conditions associated with particular purification systems (see links in side bar near the end of this page). Nevertheless, the general principles involved are the same for all ligand-target binding systems, and these concepts are the focus of this overview.90003 90004 90018 Protein Preparation Handbook 90019 90002 This 32-page handbook provides useful information on our broad portfolio of reagents and tools for protein extraction, clean-up, immunoprecipitation and purification.Practical information, selection guides, and relevant data are included to help you improve your protein yield and downstream analysis. 90003 90002 Specific topics covered included the following: 90003 90024 90025 Cell lysis and fractionation 90026 90025 Protein dialysis and other purification techniques 90026 90025 Immunoprecipitation and pull-down assays 90026 90025 Other methods for protein preparation 90026 90033 90002 Download the Protein Preparation Handbook 90003 90036 90018 How affinity purification works 90019 90002 Affinity purification generally involves the following steps: 90003 90041 90025 Incubate crude sample (e.g., cell lysate or serum) with the affinity support to allow the target molecule in the sample to bind to the immobilized ligand. 90026 90025 Wash away non-bound sample components from the support using appropriate buffers that maintain the binding interaction between target and ligand. 90026 90025 Elute (dissociate and recover) the target molecule from the immobilized ligand by altering the buffer conditions so that the binding interaction no longer occurs. 90026 90048 90002 90050 90003 90002 90053 90012 Small scale affinity purification using an antibody immobilized to a solid support.90013 Chromatography has three main components: the mobile phase or solvent containing proteins, the stationary or solid phase also called the medium or resin (which may be agarose or other porous resin) and the chromatography column. Affinity chromatography is very selective and provides high resolution with an intermediate to high sample loading capacity. The protein of interest is tightly bound to the resin under conditions that favor specific binding to the ligand, and unbound contaminants are washed off.The bound protein is then recovered in a highly purified form by changing conditions to favor elution. Elution conditions may be specific, such as a competitive ligand, or nonspecific, such as changing pH, ionic strength, or polarity. The target protein is eluted in a purified and concentrated form. 90056 90003 90004 90002 A single pass of a serum or cell-lysate sample through an affinity column can achieve greater than 1000-fold purification of a specific protein so that only a single band is detected after gel electrophoresis (e.g., SDS-PAGE) analysis. 90003 90002 Most commonly, ligands are immobilized or «coupled» directly to solid support material by formation of covalent chemical bonds between particular functional groups on the ligand (eg, primary amines, sulfhydryls, carboxylic acids, aldehydes) and reactive groups on the support (see related article on Covalent Immobilization). However, indirect coupling approaches are also possible. For example, a glutathione S-transferase (GST) -tagged fusion protein can be first captured to a glutathione support via the glutathione-GST affinity interaction and then secondarily chemically crosslinked to immobilize it.The immobilized GST-tagged fusion protein can then be used to affinity purify binding partner (s) of the fusion protein. 90003 90002 Ligands that bind to general classes of proteins (e.g., antibodies) or commonly used fusion protein tags (e.g., Histidine tag, or His-tag) are commercially available in pre-immobilized forms ready to use for affinity purification. Alternatively, more specialized ligands such as specific antibodies or antigens of interest can be immobilized using one of several commercially available activated affinity supports; for example, a peptide antigen can be immobilized to a support and used to purify antibodies that recognize the peptide.90003 90002 90003 90004 90018 Binding and elution buffers for affinity purification 90019 90002 Most affinity purification procedures involving protein: ligand interactions use binding buffers at physiologic pH and ionic strength, such as phosphate buffered saline (PBS).This is especially true when antibody: antigen or native protein: protein interactions are the basis for the affinity purification. Once the binding interaction occurs, the support is washed with additional buffer to remove nonbound components of the sample. Nonspecific (e.g., simple ionic) binding interactions can be minimized by adding low levels of detergent or by moderate adjustments to salt concentration in the binding and / or wash buffer. Finally, elution buffer is added to break the binding interaction and release the target molecule, which is then collected in its purified form.90003 90002 Elution buffers dissociate binding partners by extremes of pH (low or high), high salt (ionic strength), the use of detergents or chaotropic agents that denature one or both of the molecules, removal of a binding factor or competition with a counter ligand . In most cases, subsequent dialysis or desalting is required to exchange the purified protein from elution buffer into a more suitable buffer for storage or downstream analysis. 90003 90002 The most widely used elution buffer for affinity purification based on protein interactions is 0.1 M glycine • HCl, pH 2.5-3.0. This buffer effectively dissociates most protein: protein and antibody: antigen binding interactions without permanently affecting protein structure. However, some antibodies and proteins are damaged by low pH, so eluted protein fractions are best neutralized immediately by addition of 1 / 10th volume of alkaline buffer such as 1 M Tris • HCl, pH 8.5. Other elution buffers for affinity purification of proteins are listed in the table below. 90003 90002 90003 90078 Learn more 90079 90024 90025 Tech Tip # 27: Optimize elution conditions for affinity purification 90026 90033 90004 90018 Common elution buffer systems for protein affinity purification 90019 90002 These conditions apply primarily to protein-protein binding interactions, such as between an antibody and its peptide antigen.Elution buffers for binding interactions between other kinds of molecules may be quite different. 90003 90089 90090 90091 90092 90012 Condition 90013 90095 90092 90012 Buffer 90013 90095 90100 90091 90102 90012 pH 90013 90105 90106 90102 100 mM glycine • HCl, pH 2.5-3.0 90105 100 mM citric acid, pH 3.0 90105 50-100 mM triethylamine or triethanolamine, pH 11.5 90105 150 mM ammonium hydroxide, pH 10.5 90106 90100 90091 90102 90012 Ionic strength 90105 and / or 90105 Chaotropic effects 90013 90106 90102 3.5-4.0 M magnesium chloride, pH 7.0 in 10mM Tris 90105 5 M lithium chloride in 10mM phosphate buffer, pH 7.2 90105 2.5 M sodium iodide, pH 7.5 90105 0.2-3.0 M sodium thiocyanate 90106 90100 90091 90102 90012 Denaturing 90013 90106 90102 2-6 M guanidine • HCl 90105 2-8 M urea 90105 1% deoxycholate 90105 1% SDS 90106 90100 90091 90102 90012 Organic 90013 90106 90102 10% dioxane 90105 50% ethylene glycol, pH 8-11.5 (also chaotropic) 90106 90100 90091 90102 90012 Specific competitor 90013 90106 90102> 0.1 M counter ligand or analog 90105 (e.g., using glutathione to elute GST-tagged proteins from immobilized glutathione agarose resin) 90106 90100 90155 90156 90078 Learn more 90079 90024 90025 Tech Tip # 29: Degas solutions for use in affinity and gel filtration columns 90026 90033 90004 90002 Solid supports for affinity purification 90003 90002 Affinity purification involves the separation of molecules in solution (mobile phase) based on differences in binding interaction with a ligand that is immobilized to a stationary material (solid phase).A support or matrix in affinity purification is any material to which a biospecific ligand is covalently attached. Typically, the material to be used as an affinity matrix is ​​insoluble in the system in which the target molecule is found. Usually, but not always, the insoluble matrix is ​​a solid. Hundreds of substances have been described and utilized as affinity matrices, including agarose, cellulose, dextran, polyacrylamide, latex and controlled pore glass. Useful affinity supports are those with a high surface-area to volume ratio, chemical groups that are easily modified for covalent attachment of ligands, minimal nonspecific binding properties, good flow characteristics and mechanical and chemical stability.90003 90004 90018 Porous gel supports 90019 90002 Porous supports (also called resins or gels) generally provide the most useful properties for affinity purification of proteins.These types of supports are usually sugar- or acrylamide-based polymer resins that are produced in solution (i.e., hydrated) as 50-150 μm diameter beads. The beaded format allows these resins to be supplied as wet slurries that can be easily dispensed to fill and «pack» columns with resin beds of any size. The beads are extremely porous and large enough that biomolecules (proteins, etc.) can flow as freely into and through the beads as they can between and around the surface of the beads. Ligands are covalently attached to the bead polymer (external and internal surfaces) by various means.The result is a loose matrix in which sample molecules can freely flow past a high surface area of ​​immobilized ligand. 90003 90002 By far the most widely used matrix for protein affinity purification techniques is crosslinked beaded agarose, which is typically available in 4% and 6% densities. (This means that a 1 mL resin-bed is more than 90% water by volume.) Beaded agarose is good for routine applications as it crushes easily, making it suitable for gravity-flow, low-speed-centrifugation, and low-pressure procedures.Additional crosslinking and / or chemical hardening of beaded agarose resins can increase its ability to withstand higher pressures but can also result in lowering the binding capacity. 90003 90002 Resins based on polyacrylamide are also used as supports for column affinity chromatography. One example is Thermo Scientific UltraLink Biosupport, which does not compress as easily as typical beaded agarose. UltraLink Biosupport may be used in medium pressure applications with a peristaltic pump or other liquid chromatography systems.Both agarose and UltraLink supports have low nonspecific binding characteristics; nevertheless, they behave slightly differently in particular applications. 90003 90002 90003 90004 90018 Physical properties of affinity chromatography resins 90019 90002 Crosslinked 4% beaded agarose and crosslinked 6% beaded agarose are commonly abbreviated as agarose CL-4B and agarose CL-6B, respectively.Also see table below about choosing supports based on scale of use. 90003 90089 90090 90091 90092 90095 90092 Crosslinked 4% 90105 beaded agarose 90095 90092 Crosslinked 6% 90105 beaded agarose 90095 90092 Superflow agarose (highly crosslinked) 90095 90092 UltraLink Biosupport 90105 (acrylamide-azlactone polymer) 90095 90100 90091 90102 90012 Bead size 90105 range 90013 90106 90102 45 to 165 μm 90106 90102 45 to 165 μm 90106 90102 45 to 165 μm 90106 90102 50 to 80 μm 90106 90100 90091 90102 90012 Exclusion 90105 limit 90013 90106 90102 20,000 kDa 90106 90102 4000 kDa 90106 90102 6000 kDa 90106 90102 2000 kDa 90106 90100 90091 90102 90012 Pressure 90105 limit 90013 90106 90102 0.35 MPa 90106 90102 0.35 MPa 90106 90102 0.65 MPa 90106 90102 90002 0.69 MPa 90003 90106 90100 90091 90102 90012 Methods 90013 90106 90102 gravity-flow or low-speed centrifugation 90106 90102 gravity-flow or low-speed centrifugation 90106 90102 FPLC systems, 90105 gravity-flow 90106 90102 FPLC systems, HPLC, gravity-flow 90106 90100 90091 90102 90012 Coupling 90105 capacity 90013 90106 90102 medium 90106 90102 medium 90106 90102 medium 90106 90102 90002 high 90003 90106 90100 90091 90102 90012 pH range 90105 (tolerance) 90013 90106 90102 3-11 90106 90102 3-11 90106 90102 2-12 90106 90102 1-13 90106 90100 90155 90156 90004 90018 Magnetic particles 90019 90002 Magnetic particles are a completely different type of affinity support from beaded agarose and other porous resins.They are much smaller (typically 1-4 μm diameter) and solid (non-porous). Their small size provides the sufficient surface area-to-volume ratio needed for effective ligand immobilization and affinity purification. Magnetic beads are produced as superparamagnetic iron oxide particles that are covalently coated with silane derivatives. The coating makes the beads inert (to minimize nonspecific binding) and provides the particular chemical groups needed for attaching ligands of interest. 90003 90002 Affinity purification with magnetic particles is not performed in-column.Instead, a few microliters of beads is mixed with several hundred microliters of sample as a loose slurry. During mixing, the beads remain suspended in the sample solution, allowing affinity interactions to occur with the immobilized ligand. After sufficient time for binding has been given, the beads are collected and separated from the sample using a powerful magnet. Typically, simple bench-top procedures are done in microcentrifuge tubes, and pipetting or decanting is used to remove the sample (or wash solutions, etc.) While the magnetic beads are held in place at the bottom or side of the tube with a suitable magnet. 90003 90002 Advantages of magnetic particles over porous resins: 90003 90024 90025 Magnetic beads exhibit less non-specific binding than porous supports. 90026 90025 Magnetic beads can be used for cell separation procedures. 90026 90025 Magnetic beads are suitable for high-throughput automation. 90026 90033 90002 Magnetic beads have generally replaced agarose resin as the preferred support for assay-scale purification techniques, such as immunoprecipitation (IP) and pull-down.Furthermore, increasingly sophisticated and powerful sample-handling instruments are available for performing assays and purification procedures using magnetic separations. 90003 90004 90018 Applications and scales of use 90019 90002 The intended scale of purification and downstream application are perhaps the most important considerations when considering which type of affinity support to use.Differences in pressure limits (see table above), maximum flow rates, and factors such as cost (e.g., magnetic particles would be too costly to use at large scales) determine which support is appropriate to use in a given chromatography system. 90003 90018 Appropriate applications and scales of use for affinity chromatography supports. 90019 90089 90090 90091 90092 90095 90092 Screening or Assay 90105 Scale 90095 90092 Batch 90105 Scale 90095 90092 Pilot 90105 Scale 90095 90092 Process 90105 Scale 90095 90100 90091 90102 90012 Yield 90013 90106 90102 Microgram (μg) 90106 90102 Milligram (mg) 90106 90102 Milligram to gram 90106 90102 Gram to kilogram 90106 90100 90091 90102 90012 Technique 90013 90106 90102 Automated particle processor; 90105 96-well spin plates 90106 90102 Gravity flow; 90105 Spin columns 90106 90102 FPLC at low to medium flow rates 90106 90102 FPLC at high flow rates 90106 90100 90091 90102 90012 Applications 90013 90106 90102 High-throughput screening; 90105 intraction studies; 90105 mutational analysis; 90105 Western blot 90106 90102 Functional assays; Structural analysis 90106 90102 Structural analysis; Production scale 90106 90102 Bulk production 90106 90100 90091 90102 90012 Suitable supports 90013 90106 90393 90394 90106 90100 90155 90156 90004 90002 Types of affinity purification 90003 90002 Different classes of affinity targets, as well as different purification goals, require consideration of different priorities (e.g., high purity vs. high yield), technical limitations and buffer conditions for development of a successful procedure. The following sections describe some of the most common affinity purification systems. Links to more detailed articles about specific purification methods are provided in the gray boxes. 90003 90004 90018 Antibody purification 90019 90002 Several methods of antibody purification involve affinity purification techniques.Typical laboratory-scale antibody production involves relatively small volumes of serum, ascites fluid or culture supernatant. Depending upon how the antibody will be used for various assay and detection methods, it must be partially or fully purified. Three levels of purification specificity include the following approaches: 90003 90024 90025 90012 Precipitation with ammonium sulfate. 90013 This simple technique provides crude purification of total immunoglobulin from other serum proteins.90026 90025 90012 Affinity purification with immobilized Protein A, G, A / G or L. 90013 These proteins bind to most species and subclasses of IgG, the most abundant type of immunoglobulin produced by mammals in response to immunogens. Ready-to-use resins and purification kits with these proteins are available in many package sizes and formats. 90026 90025 90012 Affinity purification with immobilized antigen. 90013 Covalently immobilizing purified antigen (i.e., the peptide or hapten used as the immunogen to induce production of antibody by the host animal) to an affinity support allows the specific antibody to be purified from crude samples.Activated resins and complete kits for preparing immobilized antigens via a variety of chemistries are available. 90105 90026 90033 .90000 Shungite stone for water purification 90001 90002 Shungite Stone For Water Purification — What You Need To Know 90003 90004 Boiling water will cause heavy metals, salts, and nitrates to clump up, which can then cause problems to the body if continued use. The other common way of cleaning water is through the use of chlorine. This method was very popular in the past, but it is slowly being eradicated due to the fact that we now know that chlorine can result in the production of organic compounds that are linked to cancer.Using reverse osmosis is another way of cleaning water. This is method is effective and safe, but it can be costly. This is especially true if you look at the cost with a long-term perspective.Thankfully, there is a better, safer and cheaper way of cleaning water, and that is through Shungite water purification. 90005 90002 What Is Shungite Water Purification? 90003 90004 Shungite is a special type of mineral with a lot of healing properties. One of the popular ways of making use of Shungite is for cleaning water.Shungite has the ability to clean water from harmful microorganisms, bacteria, metals, organic compounds and even pesticides. The water in Lake Onega, Russia, is known to provide clean and safe drinking water that local inhabitants simply drink the water as is, without doing any disinfection process. This because the water in Lake Onega has been interacting with Shungite minerals for thousands of years. 90005 90004 The commercial use of Shungite for cleaning water started to become popular in the 1990’s.In most cases, Shungite minerals are broken down into very small pieces and incorporated into water filters. Because of Shungite’s rise in popularity, scientist began studying the mineral. After years of studies and tests, the scientist concluded that Shunite is 100% non-toxic to humans, and it can truly clean water. In fact, with sets for purification water from Shungite, there’s no need to boil water anymore to get cheap, clean and safe drinking water. Another interesting result from the studies is the discovery that Shungite has very strong anti-bacterial properties.90005 90004 According to studies, a water sample was purposely contaminated with streptococcus bacteria and other harmful microorganisms. In just half an hour, the population of streptococcus bacteria and other harmful microorganism has decreased by 90% — 100%. Shungite also has shown to clean water from iron, magnesium, nitrates, copper and chlorine compounds. It can visually clear the water and removes undesirable tastes. Also, because of the healing properties of Shungite, it’s been used to help deal with a variety of illnesses.90005 90004 90015 Shungite Water Can Help Deal With: 90016 90005 90018 90019 Allergies; 90020 90019 Anemia; 90020 90019 Gastritis; 90020 90019 Asthma; 90020 90019 Impotence; 90020 90019 Dyspepsia; 90020 90019 Liver Diseases; 90020 90019 Kidney Diseases; 90020 90019 Gall-bladder problems; 90020 90019 Diabetes. 90020 90039 90004 90005 90004 Keep in mind that Shungite water can be used internally and externally. Shungite Internal Use Drinking 2 to 3 glasses of Shungite each day may result to: 90005 90018 90019 Decrease in histamine levels in the blood; 90020 90019 Cure Acne; 90020 90019 Prevent neural, muscular or digestive problems; 90020 90019 Decrease in arthritis onsets; 90020 90019 Decrease of varicose veins.90020 90039 90056 External Use of Shungite 90057 90004 External use means the application of Shungite water on the skin, which can then help in: 90005 90018 90019 Improving Skin Elasticity; 90020 90019 Repairing various skin problems; 90020 90019 Reducing hair loss; 90020 90019 Fighting dandruff; 90020 90019 Strengthening hair roots If this your first time hearing about. 90020 90039 90004 90005 90004 90005 90004 90005.90000 definition of purification by The Free Dictionary 90001 The god had commanded that their purification should be the purification by pilgrimage.Resentment — why, it is purification; it is a most stinging and painful consciousness! Through all these means of purification for the priestly career, he passed at last into the one sphere that was worthy of him: he entered the Church, under the protection of influential friends.He immediately set about a thorough purification. Making a rude sweating-house on the banks of the river, he would shut himself up until in a reeking perspiration, and then suddenly emerging, would plunge into the river.A startling «Hi-hi!» from our camp followers and a loud «Halt!» from an English gentleman in the party checked the adventurer, and then we were informed that so dire a profanation is it for a Christian dog to set foot upon the sacred threshold of a Moorish mosque that no amount of purification can ever make it fit for the faithful to pray in again.Only by the inner purification of myself can I retain in some degree of purity the liquid I receive. «If Jesus was right, then these two unfortunates were my sisters, and the only hope of their purification was in my affection and tenderness.Near its southern termination, it received the contributions of another lake, whose waters were so limpid as to have been exclusively selected by the Jesuit missionaries to perform the typical purification of baptism, and to obtain for it the title of lake «du Saint Sacrement. » The less zealous English thought they conferred a sufficient honor on its unsullied fountains, when they bestowed the name of their reigning prince, the second of the house of Hanover .— or a polluted soul towards their purification? And as for the people’s reverence, would that it were turned to scorn and hatred! In one instance a considerable and characteristic section can be traced from extant fragments and notices: Salmoneus, son of Aeolus, had a daughter Tyro who bore to Poseidon two sons , Pelias and Neleus; the latter of these, king of Pylos, refused Heracles purification for the murder of Iphitus, whereupon Heracles attacked and sacked Pylos, killing amongst the other sons of Neleus Periclymenus, who had the power of changing himself into all manner of shapes.’I did not,’ sobbed the youth, escaping from my hands, and finishing the remainder of the purification with his cambric pocket- handkerchief.Without pondering in detail upon the matter at all, his sensations were of purification and uplift. .90000 Surface area of ​​a sphere 90001 Surface area of ​​a sphere — Math Open Reference 90002 Definition: The number of square units that will exactly cover the surface of a sphere. 90003 90002 Try this Drag the orange dot to adjust the radius of the sphere and note how the area changes. 90003 90002 90007 The surface area of ​​a sphere is given by the formula Where r is the radius of the sphere. In the figure above, drag the orange dot to change the radius of the sphere and note how the formula is used to calculate the surface area.90003 90002 This formula was discovered over two thousand years ago by the Greek philosopher Archemedes. He also realized that the surface area of ​​a sphere is exactly equal to the area of ​​the curved wall of its circumscribed cylinder, which is the smallest cylinder that can contain the sphere. See Surface area of ​​a cylinder. 90003 90011 If you know the surface area 90012 90002 By rearranging the above formula you can find the radius: where a is the surface area. 90003 90011 Interesting facts 90012 90017 90018 For a given volume, the sphere is the shape that has the smallest surface area.This why it appears in nature so much, such as water drops, bubbles and planets. 90019 90018 The surface area of ​​a sphere is exactly four times the area of ​​a circle with the same radius. You can see this in the area formula, since the area of ​​a circle is and the surface area of ​​a sphere is 90019 90022 90011 Things to try 90012 90017 90018 90027 90018 In the figure above, click «hide details». 90019 90018 Drag the orange dot to resize the sphere. 90019 90018 Calculate the volume of the sphere 90019 90018 Click «show details» to check your answer.90019 90036 90019 90018 90027 90018 In the figure above, click «reset» then uncheck «show radius» 90019 90018 Drag the orange dot to resize the sphere. 90019 90018 Calculate the radius of the sphere from the volume 90019 90018 Click «show radius» to check your answer. 90019 90036 90019 90022 90011 Related topics 90012 90002 (C) 2011 Copyright Math Open Reference. 90007 All rights reserved 90003 .