2019 KSFE Product Catalogue

Total Page:16

File Type:pdf, Size:1020Kb

2019 KSFE Product Catalogue Laboratory Chemicals 209 Description Brand Reference Packing Acacia powder, “Biochem”. R&M 2924-00 500g Acenaphthene, C.P. R&M 0003-00 500g ACES, “Biochem”. [N-(Acetomido)-2-aminoethanesulfonic acid] R&M 2340-00 25g Acetamide, C.P. (Ethanamide) R&M 0004-00 500g Acetanilide, A.R. (N-Phenylacetamide) R&M 0006-50 500g Acetate Buffer, for chlorine (pH-4), “READIL”. R&M 1560-00 500ml Acetate Buffer, pH-5.50, “READIL”. R&M 1560-55 500ml Acetic Acid, glacial, A.R. (Ethanoic acid) R&M 1410-58 2.5Lt Acetic Acid, 95%, A.R. (Ethanoic acid) R&M 1410-59 2.5Lt Acetic Acid, 5% (W/V), "READIL”. (Vinegar) R&M 1411-05 1Lt Acetic Acid, 10% (W/V), "READIL”. R&M 1411-10 1Lt Acetic Acid, 30% (W/V), "READIL”. R&M 1410-53 1Lt Acetic Acid, 50% (W/V), "READIL”. R&M 1410-50 1Lt Acetic Acid, 0.05mol/l (0.05), "READIL”. R&M 1410-51 1Lt Acetic Acid, 0.1mol/l (0.1), "READIL”. R&M 1410-52 1Lt Acetic Acid, 0.5mol/l (0.5), "READIL”. R&M 1410-53 1Lt Acetic Acid, 1.0mol/l (1.0), "READIL”. R&M 1410-54 1Lt Acetic Alcohol, “READIL”. R&M 1410-30 1Lt Acetoacetanilide, C.P. R&M 5298-50 500g Aceto-Carmine, “Biochem”. R&M 0063-80 100ml Aceto-Orcein, “Biochem”. (Connective tissue stain) R&M 0299-80 100ml Acetone, A.R. R&M 1412-50 2.5Lt Acetone, C.P. R&M 9108-50 2.5Lt Acetone, HPLC. R&M 9108-20 2.5Lt Acetone:Alcohol, “READIL”. R&M 1401-55 500ml Acetonitrile, A.R./ACS. (Methyl Cyanide) R&M 0021-51 2.5Lt Acetonitrile, HPLC. R&M 0021-30 2.5Lt Acetophenone, C.P. R&M 6879-50 500ml Acetylacetone, A.R. (2,4-Pentanedione) R&M 0027-70 500ml Acetylenetetrabromide. (1,1,2,2-Tetrabromoethane) R&M 5706-70 500ml N-Acetyl-L-Cysteine. "Biochem" R&M 5657-00 10g o-Acetylsalicylic acid, C.P.(Aspirin) R&M 4298-70 500g N-Acetyl-DL-Tryptophan. "Biochem" R&M 5807-12 25g Acid Alcohol, “READIL”. R&M AA001-60 1Lt Acid-Fast Staining Kit.(Ziehl-Neelsen Method)(AFS) - Set of 3 items R&M 6210-83 1 set Acid Fuchsin, C.I.42685, “RMstain”. R&M 2395-00 25g Acidified Methanol.(0.01% HCl). "READIL" R&M 3418-01 1Lt Acidified Molybdate, “READIL”. (Silicate Reagent A) R&M 8118-50 500ml Acridine orange, C.I.46005, “RMstain”. (For Electrophoresis) R&M 6941-00 10g Acriflavin. "Biochem" R&M 0600-36 25g Acrylamide, A.R. R&M 0076-60 500g Acrylamide, for Electrophoresis. R&M 0077-60 100g Acrylamide,4X crystallised, for Molecular Biology. R&M 0078-60 100g 30% Acrylamide/Bis-acrylamide. (for electrophoresis) R&M 0077-30 1Lt 40% Acrylamide/Bis-acrylamide. (for electrophoresis) R&M 0077-40 1Lt Acrylic Acid, C.P. R&M 6226-50 500ml Acrylonitrile, stabilised, C.P. R&M 0225-60 500ml 210 Laboratory Chemicals Description Brand Reference Packing Adenine, “Biochem”. R&M 0036-70 10g 3 Adenine Sulfate, A.R. R&M 6603-70 10g 4 Adenosine. "Biochem" R&M 6700-00 5g 320.00 Adenosine-5'-Diphosphoric acid Trisodium salts. "Biochem" R&M 6801-00 1g 520.00 Adenosine-5'-Monophosphoric acid sodium salts. "Biochem" R&M 6901-00 5g 490.00 Adenosine-5'-Triphosphoric acid disodium salts. "Biochem" R&M 7001-00 5g 4 Adipic acid, pure. R&M 0050-00 500g 1 Adonitol, “Biochem”. R&M 0054-00 10g 5 L-Adrenaline, A.R. R&M 7304-12 1g 1, L-Adrenaline Bitartrate, A.R. R&M 7304-00 5g 1,670.00 Aesulin, C.P. R&M 0081-00 5g 490.00 Agar-Agar, “Biochem”. R&M 9829-00 500g Agarose, Type A R&M 0793-00 100g 3,750.00 Agarose, Type B R&M 0794-00 100g 3,1 Agarose, Eletrophoresis (Low) R&M 0208-00 100g 4, Agarose, Eletrophoresis (Medium) R&M 0207-00 100g 4,040.00 Agarose, Eletrophoresis (High) R&M 0206-00 25g 4,040.00 6x Agarose Gel Loading Dye. R&M 9883-55 200ml 350.00 DL-Alanine, “Biochem”. R&M 0373-00 100g 520.00 L-Alanine, “Biochem”. R&M 0383-00 100g 5 Albert stain, No:A, “RMstain”. R&M 0498-00 500ml 8 Albert stain, No:B, “RMstain”. R&M 0499-00 500ml 7 Albumin, “Biochem”. R&M 4422-01 250g Albumin, Mayer's “Biochem”. R&M 4422-01 100ml Albumin, “Biochem”. R&M 4422-01 250g Albumin, Mayer's “Biochem”. R&M 4422-01 100ml Alcian Blue 8Gx, for microscopy. R&M 0830-00 5g 740.00 Alcian Blue 8Gx, 1% w/v staining soln. pH 1.2."RMStain" R&M 0830-01 100ml 470.00 Alcian Blue Staining Kit (Set of 2 items) R&M 0830-00kit 1 kit 1, Alcohol, Absolute 99.7% (Denatured). A.R. R&M CA001-50 2.5Lt Alcohol, Absolute 99.8% (Undenatured). A.R. R&M S001-50 2.5Lt 4 Alcohol, 95%. (Undenatured). A.R. R&M S9501-50 2.5Lt 370.00 Alcohol, 95%. (Denatured). A.R. R&M CA9501-50 2.5Lt Alcohol, 95% (Denatured). C.P. R&M CD9501-50 2.5Lt 70.00 Alcohol, 96% (Denatured). C.P. R&M DP9601-52 2.5Lt 7 Alcohol, 90% (V/V), "READIL". R&M DP9501-59 1Lt 48.00 Alcohol, 80% (V/V), "READIL". R&M DP9501-58 1Lt 42.00 Alcohol, 70% (Denatured). A.R. R&M C9701-90 2.5Lt 8 Alcohol, 30% (V/V), "READIL". R&M CA9501-30 1Lt Alcohol, 1% (V/V), "READIL". R&M CA9501-51 1Lt 40.00 Alcoholic Silver Nitrate soln. "READIL" (2% in Ab. Alcohol) R&M 6524-20 500ml 2 Aliginic acid, C.P. R&M 0315-00 500g 400.00 Alizarin, pH Indicator, C.I. 58000, “RMstain”. R&M 9781-00 25g Alizarin, 0.1% Alcoholic Solution, "RMstain”. R&M 9781-01 500ml 40.00 Alizarine Complexone, "RMInd" R&M 8509-00 1g 300.00 Alizarine Cyanine Green, C.I.61570, "RMStain" R&M 8526-00 25g 2 Laboratory Chemicals 211 Description Brand Reference Packing Alizarin red S, C.I. 58005, “RMstain”. R&M 9872-00 25g 90.00 Alizarin red S, 1% Indicating solution, “RMstain”. R&M 9872-10 500ml 90.00 Alizarin red S Staining Kit for Calcium (Set of 4 items) R&M 9872-00kit 1 kit 840.00 Alizarin yellow 2G (Alizarin yellow G), C.I. 14025, “RMstain”. R&M 9830-00 5g 2 Alizarine yellow R(G) “RMstain”. R&M 2243-76 25g Alkali Blue 6B, C.I. 42765, “RMstain”. R&M 0497-00 5g 520.00 Alkaline Citrate solution. "READIL" (Ammonium Test) R&M 1564-21 500ml Alkaline Iodide-Azide reagent. "READIL"(for dissolved Oxygen) R&M 5011-61 500ml 300.00 Alkaline Tartrate for Lowry Protein assay. "READIL" R&M 6803-21 1Lt 2 Allantoin, C.P. R&M 0372-00 100g 320.00 Alloxan, hydrated C.P. R&M 0870-00 25g 350.00 Allure Red. C.I.16035. "RMstain" R&M 4914-20 50g 320.00 Allyl Alcohol, C.P. R&M 8754-50 500ml Allyl Bromide, C.P. (3-Bromo-1-propene) R&M 0509-87 250ml 720.00 Allyl Chloride, C.P. (3-Chloro-1-propene) R&M 0519-87 500ml 3 Allylthiourea, C.P. R&M 3377-90 100g 1,2 Aluminium, AAS standard soln. 1000mg/l R&M 0045-30 500ml 1, Aluminium, fine powder , C.P. R&M 8912-30 500g 7 Aluminium Foil, 30x800cm, Thickness 0.01mm, C.P. R&M 8118-00 1 roll 70.00 Aluminium Sheet, 30x60cm, Thickness 7mm, C.P. R&M 8119-00 1 sheet 70.00 Aluminium Strip, 2cm x 10cm x0.2mm C.P. R&M 8119-22 5pcs/set 70.00 Aluminium Acetate, basic, A.R. R&M 2017-00 500g Aluminium Ammonium Sulphate, A.R. R&M 6775-00 1Kg Aluminium Chloride, 6-Hydrate, A.R. R&M 8005-90 500g Aluminium Fluoride, C.P. R&M 2005-80 500g Aluminium Hydroxide, C.P. R&M 9833-00 500g 5 Aluminium Iso-propoxide, C.P. R&M 0912-00 500g 2 Aluminium Nitrate, 9-Hydrate, A.R. R&M 6647-25 500g 50.00 Aluminium Oxide, A.R. R&M 8007-00 500g Aluminium Oxide, C.P. R&M 0212-00 500g 4 Aluminium Oxide, neutral, for TLC. R&M 2095-00 500g 350.00 Aluminium Oxide, active neutral, for C.C. R&M 2015-00 500g Aluminium Oxide, active acidic, for C.C . R&M 2019-00 500g Aluminium Oxide, active basic, for C.C. R&M 2018-00 500g Aluminium Oxide, G, for TLC . R&M 2011-00 500g 290.00 Aluminium Phosphate, C.P. R&M 2010-00 500g 520.00 Aluminium Potassium Sulfate, A.R./ACS. R&M 6794-00 1Kg 72.00 Aluminium Stearate, C.P. R&M 2012-00 500g Aluminium Sulfate, 30% (W/V), "READIL". R&M 6776-30 1Lt 4 Aluminium Sulfate, 40% (W/V), "READIL". R&M 6776-40 1Lt 48.00 Aluminium Sulfate, Hydrate, A.R./ACS. R&M 6776-00 1Kg Aluminon, A.R. (Aurin tricarboxylic acid ammonium salt) R&M 6924-70 25g 170.00 Amaranth (Acid Red 27), C.I.16185, “RMstain”. R&M 0193-00 25g 88.00 Amberlite Resin. (IRA-400Cl) (Strongly basic anion exchanger) R&M 55005 500g 370.00 Amberlite Resin. (IRA-120 a) (Strongly acidic cation exchanger) R&M 55009 500g 320.00 Amido black 10B , C.I.20470, “RMstain”. R&M 0319-00 25g 4-Aminoacetanilide, C.P.
Recommended publications
  • Detailed Teacher Instructions: Inheritance, X-Linkage, Evolution Over Multiple Generations, Genetic Hitchhiking
    Revised Laboratory on Molecular Evolution Gredler et al. (2015) Detailed Teacher Instructions: Inheritance, X-linkage, Evolution over Multiple Generations, Genetic Hitchhiking Objectives: Between the laboratory exercise and the associated lectures, students will be able to: Explain the process of evolution by natural selection in terms of fitness-related traits and allele frequencies Describe the concept of X-linked inheritance Perform DNA extractions, PCR, and gel electrophoresis Analyze molecular data as a means of understanding an evolutionary process Explain the concepts of selective sweeps, hitchhiking, and linkage Materials: Drosophila melanogaster heat shock white-eyed strain 60739 Drosophila melanogaster heat shock white-eyed strain 60740 Drosophila melanogaster Zimbabwe (wild type) strain 60741 Culture vials, plugs, and food (media) for Drosophila rearing Carolina Biological FlyNap® Anesthetic Kit: 173010 (Optional but strongly preferred) CO2 anesthetization facilities for Drosophila DNA extraction buffer and proteinase-K for DNA isolation Sorting brushes "Squishing buffer" and proteinase-K for DNA isolation Equipment and reagents for polymerase chain reaction including oligonucleotides for "NEAR" and "FAR" markers Equipment and reagents for agarose gel electrophoresis Magnifying glasses Sharpie markers Custom PowerPoints and projector, if desired 1 Revised Laboratory on Molecular Evolution Gredler et al. (2015) This exercise allows students to view evolution over multiple generations, experiment with molecular techniques, and learn concepts of molecular evolution. This exercise requires considerable advance preparation (must be started approximately 6 weeks before planned class start date, with initial white- eyed fly crosses starting approximately 4 weeks before the planned class start date). The supplies and directions are listed out so that you may purchase or use supplies you already have.
    [Show full text]
  • Hiper® Protein Estimation Teaching Kit (Quantitative)
    U n z i p p i n g G e n e s P r o d u c t I n f o r m a t i o n HiPer® Protein Estimation Teaching Kit (Quantitative) Product Code: HTBC005 Number of experiments that can be performed: 5 Duration of Experiment Protocol Biuret assay: 1 hour Folin – Lowry Assay: 2 hours Bradford assay: 1 hour Storage Instructions: The kit is stable for 12 months from the date of manufacture Store all the kit contents as specified in the brochure 1 Registered Office : Commercial Office 23, Vadhani Industrial Estate,LBS Marg, A-516, Swastik Disha Business Park, Tel: 00-91-22-6147 1919 15 WHO Mumbai - 400 086, India. Via Vadhani Indl. Est., LBS Marg, Fax: 6147 1920, 2500 5764 GMP Tel. : (022) 4017 9797 / 2500 1607 Mumbai - 400 086, India Email : [email protected] CERTIFIED Fax : (022) 2500 2286 Web : www.himedialabs.com The information contained herein is believed to be accurate and complete. However no warranty or guarantee whatsoever is made or is to be implied with respect to such information or with respect to any product, method or apparatus referred to herein Index Sr. No. Contents Page No. 1 Aim 3 2 Introduction 3 3 Materials Required But Not Provided 3 4 Storage 3 5 Biuret Assay 3 Principle Kit contents Important Instructions Procedure Observation and Result Interpretation 6 Folin – Ciocalteau (Lowry) Assay 6 Principle Kit contents Important Instructions Procedure Observation and Result Interpretation 7 Dye Binding (Bradford) Assay 9 Principle Kit contents Important Instructions Procedure Observation and Result Interpretation 8 Troubleshooting Guide 12 2 Aim: To determine the concentration of a protein by three commonly used methods: 1.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2015/0285765 A1 Chung Et Al
    US 20150285765A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0285765 A1 Chung et al. (43) Pub. Date: Oct. 8, 2015 (54) ACTIVE TRANSPORT OF CHARGED (52) U.S. Cl. MOLECULES INTO, WITHIN, AND/OR FROM CPC. G0IN 27/44756 (2013.01); G0IN 27/44704 CHARGED MATRICES (2013.01); G0IN 27/44708 (2013.01) (71) Applicant: Massachusetts Institute of Technology, Cambridge, MA (US) (57) ABSTRACT (72) Inventors: Kwanghun Chung, Cambridge, MA (US); Sung-Yon Kim, Cambridge, MA Articles and methods for the active transport of molecules (US); Kimberly Ohn, Boston, MA (US); into, within, and/or from a matrix are generally described. In Evan Murray, Cambridge, MA (US); some embodiments, an electric field may be used to alter the Jae Hun Cho, Cambridge, MA (US) position of the molecule with respect to the matrix. The elec tric field may be used to move the molecule to a new location (73) Assignee: Massachusetts Institute of Technology, within the matrix, remove the molecule from the matrix, or Cambridge, MA (US) infuse the molecule into the matrix. For instance, the electric field may be used to move a molecule having a binding (21) Appl. No.: 14/678,660 partner within the matrix into or away from the vicinity of the binding partner. In some embodiments, the position of the (22) Filed: Apr. 3, 2015 molecule may be altered by exposing the molecule to an electrodynamic field. In some Such embodiments, the mol Related U.S. Application Data ecule exposed to the dynamic electric field may have (60) Provisional application No.
    [Show full text]
  • Journal of Undergraduate Research, Volume 9
    U.S. Department of Energy Journal of Undergraduate Research 1 http://www.scied.science.doe.gov JOURNAL EDITORS CO-EDITOR AND PROGRAM MANAGER SHANNON DUNPHY LAZO CO-EDITOR AND ALBERT EINSTEIN FELLOW LORNA T. V ÁZQUEZ PRODUCTION EDITOR DEBBIE MAYER CONSULTING EDITOR JEFFERY DILKS TECHNICAL REVIEW BOARD DIEDRE ADAMS BRENDA HAENDLER, PH.D. EINSTEIN FELLOW AAAS S&T POLICY FELLOW NATIONAL AERONAUTICS AND SPACE ADMINISTRATION BOOZ ALLEN HAMILTON AMORET L. BUNN MARK S. HANNUM, NBCT, EINSTEIN FELLOW PACIFIC NORTHWEST NATIONAL LABORATORY NATIONAL SCIENCE FOUNDATION DIVISION OF GRADUATE EDUCATION JAMES CHERRY EASTERN CONNECTICUT STATE UNIVERSITY JEFFREY A. HOLMES OAK RIDGE NATIONAL LABORATORY ALICE CIALELLA ENVIRONMENTAL SCIENCES DEPARTMENT KERA JOHNSON BROOKHAVEN NATIONAL LABORATORY EINSTEIN FELLOW NATIONAL SCIENCE FOUNDATION RAM DEVANATHAN PACIFIC NORTHWEST NATIONAL LABORATORY KIRK E. LAGORY, PH.D. ENVIRONMENTAL SCIENCE DIVISION JEFFERY DILKS ARGONNE NATIONAL LABORATORY U.S. DEPARTMENT OF ENERGY DON LINCOLN SHANNON DUNPHY LAZO FERMI NATIONAL ACCELERATOR LABORATORY PROGRAM MANAGER U.S. DEPARTMENT OF ENERGY DEBBIE MAYER U.S. DEPARTMENT OF ENERGY PAUL F. FISCHER ARGONNE NATIONAL LABORATORY JULIE MITCHELL UNIVERSITY OF WISCONSIN BRADLEY G. FRITZ PACIFIC NORTHWEST NATIONAL LABORATORY ANTHONETTE W. PEÑA, NBCT EINSTEIN FELLOW DOUGLAS FULLER NATIONAL SCIENCE FOUNDATION ARIZONA STATE UNIVERSITY KITCHKA PETROVA, PH.D., NBCT DAVID B. GEOHEGAN EINSTEIN FELLOW OAK RIDGE NATIONAL LABORATORY NATIONAL SCIENCE FOUNDATION KOHL S. GILL TORKA S. POET AAAS S&T POLICY FELLOW PACIFIC NORTHWEST NATIONAL LABORATORY U.S. DEPARTMENT OF STATE 2 U.S. Department of Energy Journal of Undergraduate Research http://www.scied.science.doe.gov TECHNICAL REVIEW BOARD TED M. POSTON KAREN SUE STINER ENERGY AND ENVIRONMENT DIRECTORATE EINSTEIN FELLOW PACIFIC NORTHWEST NATIONAL LABORATORY U.S.
    [Show full text]
  • Modified Lowry Protein Assay Kit
    INSTRUCTIONS Modified Lowry Protein Assay Kit 0389.6 23240 Number Description 23240 Modified Lowry Protein Assay Kit, sufficient reagents for 480 test tubes or 2400 microplate assays Kit Contents: Modified Lowry Protein Assay Reagent, 480mL, containing cupric sulfate, potassium iodide, and sodium tartrate in an alkaline sodium carbonate buffer 2N Folin-Ciocalteu Reagent, 50mL Albumin Standard Ampules, 2mg/mL, 10 × 1mL ampules containing bovine serum albumin (BSA) at a concentration of 2.0mg/mL in 0.9% saline and 0.05% sodium azide; store at 4°C or room temperature Storage: Upon receipt store at 4°C. Product shipped at ambient temperature in two separate packages. IMPORTANT NOTE: To comply with Department of Transportation (DOT) shipping regulations, the 2N Folin-Ciocalteu Reagent is shipped in a separate package from the remaining components. Upon receipt of both packages, components may be placed together in a single kit box for storage. Table of Contents Introduction ................................................................................................................................................................................. 1 Preparation of Standards and Folin-Ciocalteu Reagent ............................................................................................................... 2 Test Tube Procedure .................................................................................................................................................................... 2 Microplate Procedure ..................................................................................................................................................................
    [Show full text]
  • Thermo Scientific Pierce Protein Assay Technical Handbook Version 2
    Thermo Scientific Pierce Protein Assay Technical Handbook Version 2 Table of Contents Total Protein Assays Specialty Assays Quick Technical Summaries 1 Histidine-tagged Proteins 32 Thermo Scientific HisProbe-HRP Kits 32 Introduction 4 Selection of the Protein Assay 4 Antibodies 33 Selection of a Protein Standard 5 IgG and IgM Assays 33 Standard Preparation 6 Proteases 35 Standards for Total Protein Assay 7 Compatible and Incompatible Substances 9 Protease Assays 35 Compatible Substances Table 10 Glycoproteins 36 Time Considerations 12 Glycoprotein Carbohydrate Estimation Assay 36 Calculation of Results 12 Phosphoproteins 37 Thermo Scientific Pierce 660nm Protein Assay 13 Phosphoprotein Phosphate Estimation Assay 37 Overview 13 Highlights 13 Peroxides 38 Typical Response Curves 14 Quantitative Peroxide Assay 38 BCA-based Protein Assays 15 Spectrophotometers 39 Chemistry of the BCA Protein Assay 15 BioMate 3S UV-Visible Spectrophotometer 39 Advantages of the BCA Protein Assay 16 Evolution 260 Bio UV-Visible Spectrophotometer 39 Disadvantages of the BCA Protein Assay 17 Evolution 300 UV-Visible Spectrophotometer 40 BCA Protein Assay – Reducing Agent Compatible 18 Evolution Array UV-Visible Spectrophotometer 40 BCA Protein Assay 19 Micro BCA Protein Assay 20 Coomassie Dye-based Protein Assays (Bradford Assays) 21 Chemistry of Coomassie-based Protein Assays 21 Advantages of Coomassie-based Protein Assays 21 Disadvantages of Coomassie-based Protein Assays 21 General Characteristics of Coomassie-based Protein Assays 22 Coomassie Plus (Bradford)
    [Show full text]
  • Recycling of Superfine Resolution Agarose Gel
    Recycling of superfine resolution agarose gel T.-Y. Seng1,2, R. Singh3, Q.Z. Faridah2,4, S.-G. Tan4,5 and S.S.R.S. Alwee1 1Federal Land Development Authority Biotechnology Centre, FELDA Agricultural Services Sdn. Bhd., Kuala Lumpur, Malaysia 2Institute of Bioscience, Universiti Putra Malaysia, Serdang, Malaysia 3Advanced Biotechnology and Breeding Centre, Malaysian Palm Oil Board, Bandar Baru Bangi, Selangor, Malaysia 4Biology Department, Faculty of Science, Universiti Putra Malaysia, Serdang, Selangor, Malaysia 5Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia Corresponding author: T.-Y. Seng E-mail: [email protected] Genet. Mol. Res. 12 (3): 2360-2367 (2013) Received February 2, 2012 Accepted September 25, 2012 Published March 11, 2013 DOI http://dx.doi.org/10.4238/2013.March.11.1 ABSTRACT. Genetic markers are now routinely used in a wide range of applications, from forensic DNA analysis to marker-assisted plant and animal breeding. The usual practice in such work is to extract the DNA, prime the markers of interest, and sift them out by electrically driving them through an appropriate matrix, usually a gel. The gels, made from polyacrylamide or agarose, are of high cost, limiting their greater applications in molecular marker work, especially in developing countries where such technology has great potential. Trials using superfine resolution (SFR) agarose for SSR marker screening showed that it is capable of resolving SSR loci and can be reused up to 14 times, thus greatly reducing the cost of each gel run. Furthermore, for certain applications, low concentrations of agarose sufficed and switching to lithium borate buffer, instead of the conventional Tris- borate-ethylenediaminetetraacetic acid buffer, will further save time and cost.
    [Show full text]
  • Video: Cell Culture Techniques (See Website)
    1 of 11 In this module, the structure and operation of different laboratory equipment are shown, for example, centrifugation, chromatography and spectrophotometry. Some laboratory techniques, for example, preparation of buffer, gel electrophoresis and use of laboratory stains are also included. You will find yourself gaining better lab techniques after going through this module. Video: Cell Culture Techniques (see website) A buffer is a solution that can resist the change in pH when limited quantities of acid or base are added to it. It consists of a mixture of a weak acid with its conjugate base, or a weak base with its conjugate acid, at equilibrium. This combination allows the solution to neutralize the added acid/base with the conjugate base/conjugate acid, respectively. However, this characteristic only holds true within the buffer's capacity; exceeding the limit causes significant pH change. A buffer works in balancing the concentrations of acid and base to restore desired equilibrium, a principle which is governed by Le Chatelier's principle. Buffers are necessary in maintaining pH levels to prevent denaturing of proteins, and degradation of pH sensitive biomolecules that allow for biological reactions to occur consistently. - For example, carbonic acid (CH2CO3) and bicarbonate (HCO3 ) are present in blood plasma as a buffer system to maintain a pH level of 7.35-7.45 in the human body for function. When calculating pH, we are determining the negative logarithm of the concentration of protons [H+] in a solution. Strong acid/base HCl - -> H+ + Cl- Strong acid/base dissociates completely when reacted with water. The number of moles of H+ (protons) should be equivalent to the number of moles of H+ in the acid.
    [Show full text]
  • Lowry Protein Assay Kit KB-03-004 1200 Test (96 Well Plate)
    Lowry Protein Assay Kit KB-03-004 1200 test (96 well plate) Index Introduction Pag. 1 Materials Pag. 2 Assay Principle Pag. 3 Reagent Preparation Pag. 6 Assay Protocol Pag. 7 Data Analysis Pag. 10 Warranties and Limitation of Liability Pag. 11 All chemicals should be handled with care ➢ ➢ This kit is for R&D use only Introduction Lowry Protein Quantification Assay is based on Lowry method, first described in 1951. The method relies on two different reactions. The first is the formation of a copper ion complex with amide bonds, forming reduced copper in alkaline solutions. This is called a Biuret chromophore and is commonly stabilized by the addition of tartrate. The second reaction is reduction of Folin-Ciocalteu reagent (phosphomolybdate and phosphotungstate), primarily by the reduced copper-amide bond complex as well as by tyrosine, tryptophan, histidine, cystine, and cysteine residues in protein.The monovalent copper ion catalyzes the latter reaction. The reduced Folin-Ciocalteu reagent is blue and thus detectable with a spectrophotometer in the range of 500 to 750 nm. The Biuret reaction itself is not very sensitive. Using the Folin-Ciocalteu reagent to detect reduced copper makes the Lowry assay nearly 100 times more sensitive than the Biuret reaction alone. 1 Materials BQCkit Lowry Protein Quantification Assay kit KB-03-004 1200 tests contains: Product Quantity Storage Lowry Reagent A 2 bottles RT Lowry Reagent B 1 vial RT Lowry Reagent C 1 bottle RT Protein Standard* 5 vials 4ºC *This reagent is stable during 10 days at Room Temperature and is shipped in these conditions.
    [Show full text]
  • Modified Lowry Protein Assay Reagent Kit, Sufficient Reagents for 480 Test Tube Or 2,400 Microplate Assays
    INSTRUCTIONS Modified Lowry Protein 3747 N. Meridian Road P.O. Box 117 Assay Reagent Kit Rockford, IL 61105 23240 0389w Number Description 23240 Modified Lowry Protein Assay Reagent Kit, sufficient reagents for 480 test tube or 2,400 microplate assays Kit Contents: Modified Lowry Protein Assay Reagent, 480 ml, containing cupric sulfate, potassium iodide, and sodium tartrate in an alkaline sodium carbonate buffer. 2N Folin-Ciocalteu Reagent, 50 ml Albumin Standard Ampules, 2 mg/ml, 10 x 1 ml ampules containing bovine serum albumin (BSA) at a concentration of 2.0 mg/ml in 0.9% saline and 0.05% sodium azide Storage: Upon arrival store at 4°C. Product shipped at ambient temperature. Note: Discard any kit reagent that shows discoloration or evidence of microbial contamination. This product is guaranteed for one year from the date of purchase when handled and stored properly. Table of Contents Introduction..................................................................................................................................................................................1 Preparation of Standards and Folin-Ciocalteu Reagent ...............................................................................................................2 Table 1: Preparation of Diluted Albumin (BSA) Standards ........................................................................................................2 Procedure Summary (Test Tube Procedure)................................................................................................................................2
    [Show full text]
  • Protein Quantification and Qualification Application Compendium Protein Quantification Using the Nanodrop One Spectrophotometer
    Protein quantification and qualification Application compendium Protein quantification using the NanoDrop One Spectrophotometer Welcome to protein quantification and qualification e-book. Here you’ll find a compendium of useful technical documents, application notes, and protocols for measuring proteins using the Thermo Scientific™ NanoDrop™ One/OneC Microvolume UV-Vis Spectrophotometer. Scientists can use the NanoDrop One/OneC instrument to quantify the protein content in their sample using either direct or indirect measurements. An example of a direct measurement is the Protein A280 application, which calculates protein concentration based on the sample absorbance at 280 nm and the protein- and wavelength-specific extinction coefficient. Colorimetric assays are an example of an indirect measurement. The NanoDrop One/OneC Software is hardcoded with applications to measure the product of the BCA, Bradford, Lowry, and Pierce™ 660 nm reactions. Feel free to contact us at [email protected] if you have any protein quantification or qualification questions. Table of contents Blanking with high absorbing buffers such as RIPA negatively affects Protein A280 measurements ................ 3 NanoDrop One educational animations ............................................................. 6 Quantify protein and peptide preparations at 205 nm................................................... 7 On-demand webinar: Protein Sample Evaluation using the NanoDrop One UV-Vis Spectrophotometer .............10 BCA protein assay .............................................................................11
    [Show full text]
  • Thesis Fulltext.Pdf (4.757Mb)
    Design, synthesis and testing of β-strand mimics as protease inhibitors . A thesis submitted in partial fulfilment of the requirements of the degree of Doctor of Philosophy in Biochemistry at the University of Canterbury by Steve Aitken . University of Canterbury 2006 i TABLE OF CONTENTS TABLE OF CONTENTS i PUBLICATION LIST v ABSTRACT vi ABBREVIATIONS viii ACKNOWLEDGEMENTS xi CHAPTER ONE: INTRODUCTION 1.1: Introduction to peptidomimetics and proteases 1 1.2: Protease inhibitors in the clinic 2 1.3: Importance of the β-strand in protease inhibitor design 5 1.4: Calpain as the prototype protease for the testing of β-strand mimics 8 CHAPTER TWO: DESIGN AND SYNTHESIS OF ACYCLIC β-STRAND MIMICS 2.1: Current calpain inhibitors in the scientific literature 15 2.2: Use of molecular modelling to design β-strand calpain inhibitors 19 2.3: Patentability evaluation 23 2.4: Design, synthesis and testing of N-heterocyclic dipeptide aldehyde 2.5: calpain inhibitors 26 2.5: Conclusions and future work 30 CHAPTER THREE: DESIGN AND SYNTHESIS OF CONFORMATIONALLY CONSTRAINED β-STRAND MIMICS 3.1: Conformational constraint of peptidomimetics 35 3.2: History of RCM 36 3.3: Mechanism elucidation and metathesis catalyst development 37 3.4: The advent of well defined single-component catalysts 39 3.5: Design and synthesis of N-N conformationally constrained SJA analogues 48 3.6: Design and synthesis of β-amino acid C-N carbocycles 53 ii 3.7: Conclusions and future work 60 CHAPTER FOUR: DESIGN AND SYNTHESIS OF MACROCYCLIC β-STRAND MIMICS 4.1: Use of macrocyclisation
    [Show full text]