linear acrylamide (5 mg/ml) (1 ml tube)

Linear Acrylamide (5 mg/ml) (1 ml Tube)

Ambion Linear Acrylamide (5 mg/mL) is for use as a nucleic acid coprecipitant and is ideal for PCR and RT-PCR reactions since small amounts of contaminating nucleic acids present in other carriers could be amplified. It is supplied in five tubes containing 1 mL each. Ideal for RT-PCR Increases pelle

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linear polyacrylamide solution 5 mg/ml molecular biology

Linear polyacrylamide solution 5 mg/ml Molecular biology

Synonyms: LPA solution for DNA/RNA precipitation Linear polyacrylamide solution for DNA/RNA precipitation, 5mg/ml, Molecular Biology Grade. Liquid.

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linear polyacrylamide solution - bioron gmbh

Linear Polyacrylamide Solution - BIORON GmbH

Linear Polyacrylamide Solution 5 mg/ml is used as an additive in DNA or while nucleotides and oligonucleotide primers remain in the liquid phase. Linear Polyacrylamide Solution 5 mg/mL is free of animal origin. We are a producer and worldwide acting trader of molecular biological and diagnostic products since 2002.

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linear acrylamide solution (linear polyacrylamide, lpa

Linear Acrylamide Solution (Linear polyacrylamide, LPA

Usage: 1 -2μL (5-10 μg) of 5mg/mL Linear acrylamide (LPA) solution is adequate for 500 μL DNA or RNA solution. Linear polyacrylamide pellet does not stick tightly on the bottom of microfuge tube. Be careful not to discard pellet when you remove supernatant.

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lpa solution 5mg/ml - bio basic

LPA Solution 5mg/ml - Bio Basic

Product Description: Linear Poly Acrylamide Solution (5mg/ml): The purification of nucleic acids for PCR, RT-PCR and other enzymatic reactions by alcohol precipitation is an essential step to yield high-quality results. Traditional alcohol precipitation procedures require co-precipitants like glycogen or yeast RNA to improve the recovery of nucleic acids.

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linear acrylamide solution (5 mg/ml)

Linear Acrylamide Solution (5 mg/mL)

上海翊圣生物科技有限公司 客服热线:400-6111-883 E-mail: order@yeasen.com 本产品仅作科研用途! 第1 页,共1 页 HB181207 Linear Acrylamide Solution (5 mg/mL) 线性化丙烯酰胺溶液(5 mg/mL) 产品信息

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linear polyacrylamide solution | bioron gmbh

Linear Polyacrylamide Solution | BIORON GmbH

Linear Polyacrylamide Solution Linear polyacrylamide is used as an additive in DNA or RNA solutions for the improvement of nucleic acids recovery during alcohol precipitation. Fragments larger than 20 bases can be precipitated in picogramm amounts, while nucleotides and oligonucleotide primers remain in the liquid phase.

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preparation of linear polyacrylamide - 实验方法 - 丁香通

Preparation of linear polyacrylamide - 实验方法 - 丁香通

5.Recover the polymer by centrifugation,and dissolve the pellet in10 mM Tris-HCl (pH8.0),1 mM EDTA to make a final polyacrylamide concentration of 5 mg/ml. 6.The linear polyacrylamide solution can be stored in the refrigerator for several years.

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ace-inhibitory peptides from bovine caseins released with

ACE-inhibitory peptides from bovine caseins released with

ACE activity was determined by incubating in a quartz cuvette 3 μL of ACE (1 U, Sigma) with 2 μL of fluorescent-substrate solution in dimethyl-sulfoxide vehicle (at 0.5 mg/100 mL) in the presence of 25 μL of the hydrolysate sample in a total volume of 3 mL of 0.1 M Tris-HCl buffer (pH 7.0) containing 50 mM NaCl and 10 mM zinc chloride at 37 °C.

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analysis of thylakoid membrane protein complexes by blue

Analysis of Thylakoid Membrane Protein Complexes by Blue

Large multisubunit protein complexes photosystem PSI and PSII, Cyt b 6 f and ATPase coordinate the production of NADPH and ATP in photosynthetic light reactions. In higher plant chloroplasts, the complexes are located in the thylakoid membrane, which is a structurally heterogeneous membrane structure, comprising appressed grana and non-appressed stroma thylakoids.

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expression of recombinant glutamic - scientific reports

Expression of recombinant glutamic - Scientific Reports

The expression of GAD65 was first evaluated at different MOI (0.5, 1, 2, 4 and 8 pfu per cell) on 6 × 10 5 Sf9 cells/mL. After infection, cells were incubated in the dark at 27 °C.

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the journal of vol. 267, no. 13, hue of may 5, pp. 923

THE JOURNAL OF Vol. 267, No. 13, hue of May 5, pp. 923

THE JOURNAL OF BIOLOGICAL CHEMISTRY 0 1992 by The American Society for Biochemistry and Molecular Biology, Inc. Vol. 267, No. 13, hue of May 5, pp. 923&9240,1992 Printed in U.S.A. Purification to Apparent Homogeneity and Partial Characterization of Rat Liver UDP-G1ucose:Glycoprotein Glucosyltransferase* (Received for publication, November 25, 1992)

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gel electrophoresis chromatography chemicals | spectrum

Gel Electrophoresis Chromatography Chemicals | Spectrum

Spectrum carries a selection of gel electrophoresis chemicals used in analytical and preparative separation techniques for large molecules such as DNA, RNA and proteins. The method enables the sorting of macromolecules by size using the electromotive force used to move the molecules through a gel matrix.

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structure and interactions of fish type iii antifreeze

Structure and Interactions of Fish Type III Antifreeze

It has been suggested that above a critical protein concentration, fish Type III antifreeze protein (AFP III) self-assembles to form micelle-like structures that may play a key role in antifreeze activity. To understand the complex activity of AFP III, a comprehensive description of its association state and structural organization in solution is necessary. We used analytical

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investigation of biological property of nanohydroxyapatite

Investigation of Biological Property of Nanohydroxyapatite

The biological effects of nanohydroxyapatites and its cell toxicity have been studied using the MTT and ALP method, infrared spectrum of absorption and electrophoresis method, respectively. The nanohydroxyapatites are prepared and made by using Sol-gel method, in which the parameters of process and reaction are controlled as: pH > 9, Ca / P = 1.67, sintering temperature of 1100°C and

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the j biological c © 2004 by the american society

THE J BIOLOGICAL C © 2004 by The American Society

buffer B (50 mM Tris, 1 M NaCl, pH 8.5). The peak enriched with BLS was further purified on a Superdex-200 column with phosphate-buff-ered saline buffer, 1 mM DTT. The purity of the BLS preparation was determined on SDS-15% (w/v) polyacrylamide gels. Purified BLS was concentrated (10 mg/ml), frozen in liquid N 2, and stored at 20 °C. Circular

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sigma-aldrich: analytical, biology, chemistry & materials

Sigma-Aldrich: Analytical, Biology, Chemistry & Materials

Sigma-Aldrich is a leading Life Science and High Technology company. Our products are used worldwide to enable science that improves the quality of life.

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expression of recombinant glutamic - scientific reports

Expression of recombinant glutamic - Scientific Reports

The expression of GAD65 was first evaluated at different MOI (0.5, 1, 2, 4 and 8 pfu per cell) on 6 × 10 5 Sf9 cells/mL. After infection, cells were incubated in the dark at 27 °C.

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production of a monoclonal antibody against serum

Production of a monoclonal antibody against serum

IgM was first dialyzed against 0.5 M Tris–HCl (pH 8) and then reduced with 0.2 M 2-mercaptoethanol for 2 hr at room temperature. Iodoacetamide f was added in a concentration of 130 mg/ml, and the solution was incubated at 4°C for 30 min. Then, the µ-heavy chain was separated by SEC.g The purity of these fractions was analyzed by 10% SDS-PAGE,

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protein purification support—getting started | thermo

Protein Purification Support—Getting Started | Thermo

Get tips and helpful information when starting with your protein purification experiment from choosing the right purification strategy to finding the best tools for your workflow from our broad selection of resins and formats, and optimizing your experiment to get the best results.

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molecular characterization of recombinant human interferon

Molecular Characterization of Recombinant Human Interferon

This product is presented as a lyophilized powder, formulated with 1.5 mg of human serum albumin (HSA), at 1, 3, 5, 9 and 10 x 106 IU of IFN-a 2b per vial. This work presents a detailed characterization of IFN-a 2b (CIGB, Havana, Cuba) using analytical methods with the sensitivity and resolution required to evidence its quality. Finally, the

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the journal of vol. 267, no. 13, hue of may 5, pp. 923

THE JOURNAL OF Vol. 267, No. 13, hue of May 5, pp. 923

THE JOURNAL OF BIOLOGICAL CHEMISTRY 0 1992 by The American Society for Biochemistry and Molecular Biology, Inc. Vol. 267, No. 13, hue of May 5, pp. 923&9240,1992 Printed in U.S.A. Purification to Apparent Homogeneity and Partial Characterization of Rat Liver UDP-G1ucose:Glycoprotein Glucosyltransferase* (Received for publication, November 25, 1992)

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non‐labelled benzodiazepines partitioned into - deepdyve

Non‐labelled benzodiazepines partitioned into - DeepDyve

A method for the extraction and quantification by high performance liquid chromatography (HPLC) of non‐labelled benzodiazepines partitioned into biological membranes has been developed. The benzodiazepine (BZD) was partitioned in a synaptosomal membrane–buffer system. The membranous pellet was separated by centrifugation and from this pellet, previously submitted or not to a proteolytic

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blue native polyacrylamide gel electrophoresis (bn-page

Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE

Aldolase (158 kD) 10 mg/ mL Catalase (232 kD) 10 mg/ mL Ferritin (440 and 880 kD) 10 mg/ mL Thyroglobulin (670 kD) 10 mg/ mL BSA (66 and 132 kD) 10 mg/ mL Bis-tris 20 mM NaCl 20 mM Glycerol 10% Adjust pH to 7.0 with HCl. Store at 4°C. Molecular weight markers are also commercially available from several sources, including Invitro-gen or

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background

Background

The company provided the complex at 1 mg/mL in 50 mM sodium citrate buffer, pH 5.5 and quality control activated. The toxin activity in mouse LD50 or units (U) of specific toxicity obtained from the provider was as follows: [3.3-3.6 × 10^6]. We acquired all chemicals from Sigma-Aldrich (Saint Louis, MO), unless otherwise stated.

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(iucr) a three-domain copper-nitrite reductase with a

(IUCr) A three-domain copper-nitrite reductase with a

Samples of protein equivalent to 0–50 µ M Cu (275 µl) were added of 250 µl biquinoline solution (5 mg ml −1 in glacial acetic acid) and 225 µl of 20 m M ascorbic acid in phosphate buffer pH 6.0 in sequential order. The reaction mixture was maintained at room temperature for 10 min and the absorbance at 546 nm was measured.

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production of a monoclonal antibody against serum

Production of a monoclonal antibody against serum

IgM was first dialyzed against 0.5 M Tris–HCl (pH 8) and then reduced with 0.2 M 2-mercaptoethanol for 2 hr at room temperature. Iodoacetamide f was added in a concentration of 130 mg/ml, and the solution was incubated at 4°C for 30 min. Then, the µ-heavy chain was separated by SEC.g The purity of these fractions was analyzed by 10% SDS-PAGE,

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mechanism of dna lesion homing and recognition by the uvr

Mechanism of DNA Lesion Homing and Recognition by the Uvr

The 5′ end labeled UvrB-dsDNA complexes (2 nM) were then incubated with 5-100 nM UvrC in 50 mM Tris pH 7.4, 100 mM NaCl, 0.1 mg/ml BSA, 1 mM ATP, 10 mM MgCl 2, and 5% (v/v) glycerol at 55°C for 30 minutes. Reactions were terminated by adding an equal volume of a stop buffer (20 mM EDTA, 95% formamide, 0.05% bromophenol blue, and 0.05% xylene

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molecular characterization of recombinant human interferon

Molecular Characterization of Recombinant Human Interferon

This product is presented as a lyophilized powder, formulated with 1.5 mg of human serum albumin (HSA), at 1, 3, 5, 9 and 10 x 106 IU of IFN-a 2b per vial. This work presents a detailed characterization of IFN-a 2b (CIGB, Havana, Cuba) using analytical methods with the sensitivity and resolution required to evidence its quality. Finally, the

Get Price
protein purification support—getting started | thermo

Protein Purification Support—Getting Started | Thermo

Get tips and helpful information when starting with your protein purification experiment from choosing the right purification strategy to finding the best tools for your workflow from our broad selection of resins and formats, and optimizing your experiment to get the best results.

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ph on structure and function of amaranth protein isolates

pH on Structure and Function of Amaranth Protein Isolates

pH on Structure and Function of Amaranth Protein Isolates. September 27/ September 2010 - October 2010Cereal Chemistry - pg. 448 Vol. 87 No. 5 ISSN: 0009-0352 -- Structural and functional properties of two amaranth protein isolates as a function of pH were studied. Isolates. A9 and All, were obtained by alkaline extraction at pH 9 and 11, respectively.

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cyanohydrin phosphonate natural product from streptomyces

Cyanohydrin Phosphonate Natural Product from Streptomyces

Streptomyces regensis strain WC-3744 was identified as a potential phosphonic acid producer in a large-scale screen of microorganisms for the presence of the pepM gene, which encodes the key phosphonate biosynthetic enzyme phosphoenolpyruvate phosphonomutase. 31P NMR revealed the presence of several unidentified phosphonates in spent medium after growth of S. regensis.

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