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Pest Management Strategic Plan for Strawberry Production in California
PEST MANAGEMENT STRATEGIC PLAN FOR STRAWBERRY PRODUCTION IN CALIFORNIA 1 | Page TABLE OF CONTENTS INTRODUCTION ................................................................................................................................................... 5 Previous Pest Management Strategic Plan .............................................................................................. 5 Development of the New Plan .................................................................................................................... 5 STRAWBERRY MARKET SHARE AND VALUE.................................................................................................... 10 STRAWBERRY PRODUCTION OVERVIEW ........................................................................................................ 13 PEST MANAGEMENT FOR COMMERCIAL STRAWBERRY PLANTINGS ......................................................... 22 LAND PREPARATON THROUGH PLANTING ............................................................................................... 22 Activities Prior to Fumigation................................................................................................................. 22 Soil Fumigation ........................................................................................................................................ 22 Planting ..................................................................................................................................................... 25 Work Group Recommendations for -
Proteinase K Dna Extraction Protocol
FT-85870n Proteinase K Product data Proteinase K, from Tritirachium album timber (Engyodontium album) Syn.: peptidase K, Tritirachium alkaline proteinase Protein K powder #858706 Proteinase K solution #718961 CAS: [ 39450-01-6 ] MW: 8,900 daltons (28.9 kDa). primary sequence for proteinase K: GAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEF EGRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDN GSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQ SSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVL DIFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASAC Proteinase K Protein Structure RYIADTANKGDLSNIPFGTVNLLAYNNYQA FAQ & Technical tips What is Proteinase K? PProteinase K (also protease K or endopeptidase K) is a broad-spectrum serine protease widely used in molecular biology. Proteinase K is able to digest native keratin (hair), hence, the name “Proteinase K”. It is commonly used because of its broad specificity, that makes it useful to clean nucleic acid complexe samples and to lyse cells. It has been used for isolation of mRNA, high molecular weight DNA and to inactivate other enzymatic activities. The enzyme was discovered in 1974 in extracts of the fungus Engyodontium album (formerly Tritirachium album). What are proteinase K applications? Proteinase K is ideal for many molecular biology applications because it is able to break down proteins and inactivate DNases and RNases that would otherwise degrade a desired sample of DNA or RNA. - Digestion of unwanted proteins in molecular biology applications - Removal of endotoxins bound to cationic proteins such as lysozyme and RNaseA - Removal of nucleases for in situ hybridization - Prion research with respect to TSE (transmissible spongiform encephalopathies) - Protease footprinting - Mitochontrial isolation - Isolation of genomic DNA - Isolation of cytoplasmic RNA - Isolation of highly native DNA or RNA Proteinase K is commonly used in molecular biology to digest protein and remove contamination from preparations of nucleic acid. -
Proteinase K # GE010.0100 – 100 Mg (FOR RESEARCH ONLY)
Product Info GE010 1 V6.0 – 6/2020 Proteinase K # GE010.0100 – 100 mg (FOR RESEARCH ONLY) Proteinase K is a broad-spectrum serine protease (28.9kDa monomer) that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic, and hydrophobic amino acids. Quantity 100 mg lyophilized powder purified from Pichia pastoris harbouring the gene encoding endolytic protease from Tritirachium album. Supplied with 1 ml of a 10x concentrated Storage Buffer. Applications Isolation of genomic DNA from cultured cells and tissues; removal of DNases and RNases during DNA and/or RNA purification; determination of enzyme locations. Specifications Free of DNases and RNases. Specific Activity: >30 units per mg. Quality Control Enzyme activity is assayed by digesting hemoglobin at a concentration of 16.7 mg/ml in a solution of 80mM potassium phosphate (pH 7.5), 5M urea, 4mM NaCl, 3mM CaCl2. Absence of endodeoxyribonucleases, exodeoxyribonucleases, and ribonucleases was confirmed by appropriate assays. Storage Store lyophilized powder at +4ºC for several months or -20ºC for at least 2 years. The concentrated (10x) storage buffer (500mM Tris-HCl, 50mM CaCl2) can be stored at room temperature or +4ºC. GRiSP Research Solutions 2020 Product Info GE010 2 V6.0 – 6/2020 Prior to use Reconstitute Proteinase K at a desired concentration (e.g. 10 mg/ml) using either ultrapure water or 1x Storage Buffer (50mM Tris-HCl pH8.0) [dilute storage buffer with ultrapure DNase/RNase-free water with or without glycerol (see below)]. Reconstituted Proteinase K should be stored at +4ºC for up to a few months. If longer storage is required, reconstitute Proteinase K in 1x Storage Buffer containing 50% glycerol and store at -20ºC Enzyme activity Proteinase K is activated by calcium (1-5mM). -
Effect of Aminophylline on Diaphragmatic Contractility in the Piglet
003 1-3998/90/2803-0196$02.00/0 PEDIATRIC RESEARCH Vol. 28, No. 3, 1990 Copyright 0 1990 International Pediatric Research Foundation, Inc. Printed in (I.S.A. Effect of Aminophylline on Diaphragmatic Contractility in the Piglet DENNIS E. MAYOCK, THOMAS A. STANDAERT, JON F. WATCHKO, AND DAVID E. WOODRUM1 University of Washington School of Medicine, Department of Pediatrics, Division of Neonatal and Respiratory Diseases, Seattle, Washington 98195 ABSTRACT. Minute ventilation, arterial blood gases, ar- of arterial oxygen > 8 kPa (60 torr) in room air, and a partial terial pH, cardiac output, and transdiaphragmatic force pressure of the arterial carbon dioxide 5 6.7 kPa (50 torr) were generation, both during spontaneous ventilation and in accepted for study. The animals were anesthetized with an i.v. response to phrenic nerve stiwulation during airway occlu- combination of chloralose (30 mg/kg) and urethane (1 50 mg/ sion at end expiration, were measured in nine anesthetized, kg) and studied in the supine position. Subsequent infusions of tracheostomized piglets before and 30 min after parenteral anesthetic were used if the piglet developed jaw clonus. A trache- infusion of 20 mg/kg aminophylline. Serum theophylline ostomy was placed and connected to a two-way nonrebreathing levels averaged 109 f 21 ~mol/L(19.7 f 3.7 ~g/mL)at valve (model 2384, Hans Rudolph, Inc., Kansas City, MO). 30 min postinfusion. No significant changes were noted in Inspiratory flow was detected by a hot-wire anemometer and pH, blood gases, blood Pressure, or ventilatory measures integrated to provide tidal volume. All animals breathed 50% after aminophylline. -
Aminophylline Catalog Number A1755 Storage
Aminophylline Catalog Number A1755 Storage Temperature –20 °C Replacement for Catalog Number 216895 CAS RN 317-34-0 Storage/Stability Synonyms: theophylline hemiethylenediamine complex; Aminophylline should be kept tightly closed to prevent 3,7-dihydro-1,3-demethyl-1H-purine-2,6-dione CO2 absorption from the atmosphere, which leads to compound with 1,2-ethanediamine (2:1); formation of theophylline and decreased solubility in 1,2 3 (theophylline)2 • ethylenediamine aqueous solutions. Stock solutions should be protected from light and prevented from contact with Product Description metals.2 Molecular Formula: C7H8N4O2 ·1/2 (C2H8N2) Molecular Weight: 210.3 References 1. The Merck Index, 12th ed., Entry# 485. Aminophylline is a xanthine derivative which is a 2. Martindale: The Extra Pharmacopoeia, 31st ed., combination of theophylline and ethylenediamine that is Reynolds, J. E. F., ed., Royal Pharmaceutical more water soluble than theophylline alone. Society (London, England: 1996), pp. 1651-1652. Aminophylline has been widely used as an inhibitor of 3. Data for Biochemical Research, 3rd ed., Dawson, cAMP phosphodiesterase.3 R. M. C., et al., Oxford University Press (New York, NY: 1986), pp. 316-317. Aminophylline has been shown to limit 4. Pelech, S. L., et al., cAMP analogues inhibit phosphatidylcholine biosynthesis in cultured rat phosphatidylcholine biosynthesis in cultured rat hepatocytes.4 It has been used in studies of acute hepatocytes. J. Biol. Chem., 256(16), 8283-8286 hypoxemia in newborn and older guinea pigs.5 The (1981). effect of various xanthine derivatives, including 5. Crisanti, K. C., and Fewell, J. E., Aminophylline aminophylline, on activation of the cystic fibrosis alters the core temperature response to acute transmembrane conductance regulator (CFTR) chloride hypoxemia in newborn and older guinea pigs. -
NINDS Custom Collection II
ACACETIN ACEBUTOLOL HYDROCHLORIDE ACECLIDINE HYDROCHLORIDE ACEMETACIN ACETAMINOPHEN ACETAMINOSALOL ACETANILIDE ACETARSOL ACETAZOLAMIDE ACETOHYDROXAMIC ACID ACETRIAZOIC ACID ACETYL TYROSINE ETHYL ESTER ACETYLCARNITINE ACETYLCHOLINE ACETYLCYSTEINE ACETYLGLUCOSAMINE ACETYLGLUTAMIC ACID ACETYL-L-LEUCINE ACETYLPHENYLALANINE ACETYLSEROTONIN ACETYLTRYPTOPHAN ACEXAMIC ACID ACIVICIN ACLACINOMYCIN A1 ACONITINE ACRIFLAVINIUM HYDROCHLORIDE ACRISORCIN ACTINONIN ACYCLOVIR ADENOSINE PHOSPHATE ADENOSINE ADRENALINE BITARTRATE AESCULIN AJMALINE AKLAVINE HYDROCHLORIDE ALANYL-dl-LEUCINE ALANYL-dl-PHENYLALANINE ALAPROCLATE ALBENDAZOLE ALBUTEROL ALEXIDINE HYDROCHLORIDE ALLANTOIN ALLOPURINOL ALMOTRIPTAN ALOIN ALPRENOLOL ALTRETAMINE ALVERINE CITRATE AMANTADINE HYDROCHLORIDE AMBROXOL HYDROCHLORIDE AMCINONIDE AMIKACIN SULFATE AMILORIDE HYDROCHLORIDE 3-AMINOBENZAMIDE gamma-AMINOBUTYRIC ACID AMINOCAPROIC ACID N- (2-AMINOETHYL)-4-CHLOROBENZAMIDE (RO-16-6491) AMINOGLUTETHIMIDE AMINOHIPPURIC ACID AMINOHYDROXYBUTYRIC ACID AMINOLEVULINIC ACID HYDROCHLORIDE AMINOPHENAZONE 3-AMINOPROPANESULPHONIC ACID AMINOPYRIDINE 9-AMINO-1,2,3,4-TETRAHYDROACRIDINE HYDROCHLORIDE AMINOTHIAZOLE AMIODARONE HYDROCHLORIDE AMIPRILOSE AMITRIPTYLINE HYDROCHLORIDE AMLODIPINE BESYLATE AMODIAQUINE DIHYDROCHLORIDE AMOXEPINE AMOXICILLIN AMPICILLIN SODIUM AMPROLIUM AMRINONE AMYGDALIN ANABASAMINE HYDROCHLORIDE ANABASINE HYDROCHLORIDE ANCITABINE HYDROCHLORIDE ANDROSTERONE SODIUM SULFATE ANIRACETAM ANISINDIONE ANISODAMINE ANISOMYCIN ANTAZOLINE PHOSPHATE ANTHRALIN ANTIMYCIN A (A1 shown) ANTIPYRINE APHYLLIC -
Tanibirumab (CUI C3490677) Add to Cart
5/17/2018 NCI Metathesaurus Contains Exact Match Begins With Name Code Property Relationship Source ALL Advanced Search NCIm Version: 201706 Version 2.8 (using LexEVS 6.5) Home | NCIt Hierarchy | Sources | Help Suggest changes to this concept Tanibirumab (CUI C3490677) Add to Cart Table of Contents Terms & Properties Synonym Details Relationships By Source Terms & Properties Concept Unique Identifier (CUI): C3490677 NCI Thesaurus Code: C102877 (see NCI Thesaurus info) Semantic Type: Immunologic Factor Semantic Type: Amino Acid, Peptide, or Protein Semantic Type: Pharmacologic Substance NCIt Definition: A fully human monoclonal antibody targeting the vascular endothelial growth factor receptor 2 (VEGFR2), with potential antiangiogenic activity. Upon administration, tanibirumab specifically binds to VEGFR2, thereby preventing the binding of its ligand VEGF. This may result in the inhibition of tumor angiogenesis and a decrease in tumor nutrient supply. VEGFR2 is a pro-angiogenic growth factor receptor tyrosine kinase expressed by endothelial cells, while VEGF is overexpressed in many tumors and is correlated to tumor progression. PDQ Definition: A fully human monoclonal antibody targeting the vascular endothelial growth factor receptor 2 (VEGFR2), with potential antiangiogenic activity. Upon administration, tanibirumab specifically binds to VEGFR2, thereby preventing the binding of its ligand VEGF. This may result in the inhibition of tumor angiogenesis and a decrease in tumor nutrient supply. VEGFR2 is a pro-angiogenic growth factor receptor -
7 EDTA, Tetraso
REPORT Safety Assessment of EDTA, Calcium Disodium EDTA. Diammonium EDTA, Dipotassium EDTA. 7 Disodium EDTA, TEA- EDTA, Tetrasod=um EDTA, Tripotassium EDTA, Trisodium EDTA, HEDTA and Trisodium HEDTA ABSTRACT EDTA (ethylenediamine tetraacetic acid) and its salts are substituted diamines. HEDTA (hydroxyethyl ethylenediamine triacetic acid) and its trisodium salt are substituted amines. These ingredients function as chelating agents in cosmetic formulations. The typical concentration of use of EDTA is less than 2%, with the other salts in current use at even lower concentrations. The lowest dose reported to cause a toxic effect in animals was 750 mg/kg/day. These chelating agents are cytotoxic and weakly genotoxic, but not carcinogenic. Oral exposures to EDTA produced adverse reproductive and developmental effects in animals. Clinical tests reported no absorption of an EDTA salt through the skin. These ingredients, are likely, however, to affect the passage of other chemicals into the skin because they will chelate calcium. Exposure to ED TA in most cosmetic formulations, therefore, would produce systemic exposure levels well below those seen to be toxic in oral dosing studies. Exposure to EDTA in cosmetic formulations that may be inhaled, however, was a concern. An exposure assessment done using conservative assumptions predicted that the maximum EDTA dose via inhalation of an aerosolized cosmetic formulation is below that which has been shown to produce reproductive or developmental toxicity. Because of the potential to increase the penetration of other chemicals, formulators should continue to be aware of this when combining these ingredients with ingredients that previously have been determined to be safe primarily because they were not significanUy absorbed. -
Lessons and Considerations for the Creation of Universal Primers Targeting Non-Conserved, Horizontally
bioRxiv preprint doi: https://doi.org/10.1101/2020.03.30.017442; this version posted April 1, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Lessons and considerations for the creation of universal primers targeting non-conserved, horizontally 2 mobile genes 3 4 Damon C. Brown,a Raymond J. Turnera# 5 aDepartment of Biological Sciences, University of Calgary, Calgary, Alberta, Canada 6 7 Running Head: Primer design approaches for nonconserved mobile genes 8 #Address correspondence to Raymond J. Turner, [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.03.30.017442; this version posted April 1, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 9 Abstract 10 Effective and accurate primer design is an increasingly important skill as the use of PCR-based 11 diagnostics in clinical and environmental settings is on the rise. While universal primer sets have been 12 successfully designed for highly conserved core genes such as 16S rRNA and characteristic genes such as 13 dsrAB and dnaJ, primer sets for mobile, accessory genes such as multidrug resistance efflux pumps 14 (MDREP) have not been explored. Here, we describe an approach to create universal primer sets for 15 select MDREP genes chosen from five superfamilies (SMR, MFS, MATE, ABC and RND) identified in a 16 model community of six members (Acetobacterium woodii, Bacillus subtilis, Desulfovibrio vulgaris, 17 Geoalkalibacter subterraneus, Pseudomonas putida and Thauera aromatica). -
S-Carboxymethylcysteine Synthase from Escherichia Coli
Agric. Biol. Chem., 53 (9), 2481 -2487, 1989 2481 S-Carboxymethylcysteine Synthase from Escherichia coli Hidehiko Kumagai,* Hideyuki Suzuki, Hiroki Shigematsu and Tatsurokuro Tochikura Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto 606, Japan Received April 14, 1989 An enzyme that catalyzes the synthesis of S-carboxymethyl-L-cysteine from 3-chloro-L-alanine (3-Cl-Ala) and thioglycolic acid was found in Escherichia coli W3110 and was designated as S- carboxymethyl-L-cysteine synthase. It was purified from the cell-free extract to electrophoretic homogeneity and was crystallized. The enzymehas a molecular weight of 84,000 and gave one band corresponding to a molecular weight of 37,000 on SDS-polyacrylamide gel electrophoresis. The purified enzyme catalyzed the ^-replacement reactions between 3-Cl-Ala and various thiol compounds. The apparent Kmvalues for 3-Cl-Ala and thioglycolic acid were 40mMand 15.4mM.The enzyme showedvery low activity as to the a,/^-elimination reaction with 3-Cl-Ala and L-serine. It was not inactivated on the incubation with 3-Cl-Ala. Theabsorption spectrum of the enzymeshows a maximum at 412nm, indicating that it contains pyridoxal phosphate as a co factor. The N-terminal amino acid sequence was determined and the corresponding sequence was detected in the protein sequence data bank, but no homogeneous sequence was found. 3-Chloro-L-alanine (3-Cl-Ala) acts as a so- called suicide substrate for some pyridoxal- Materials and Methods phosphate (PLP) dependent enzymes, such Reagents. Casamino acids and Tryptone were obtained as glutamate-oxaloacetic acid transminase,1} from Difco Laboratories, yeast extract from Oriental glutamate-pyruvic acid transaminase2) and Yeast Co., amido black 10B from E. -
Pullulan Ω-Carboxyalkanoates for Drug Nanodispersions Jameison T
Pullulan ω-carboxyalkanoates for Drug Nanodispersions Jameison Theophilus Rolle Thesis submitted to the faculty of the Virginia Polytechnic Institute and State University in partial fulfillment of the requirements for the degree of Master of Science In Macromolecular Science and Engineering Kevin J. Edgar, Committee Chair Richey Davis Lynne S. Taylor July 30th, 2015 Blacksburg, VA Keywords: pullulan, amorphous solid dispersions, carboxyalkanoates, drug delivery Copyright 2015, Jameison T. Rolle Pullulan ω-carboxyalkanoates for Drug Nanodispersions Jameison T. Rolle Abstract Pullulan is an exopolysaccharide secreted extracellularly by the black yeast-like fungi Aureobasidium pullulans. Due to an α-(1→6) linked maltotriose repeat unit, which interferes with hydrogen bonding and crystallization, pullulan is completely water soluble unlike cellulose. It has also been tested and shown to possess non-toxic, biodegradable, non-mutagenic and non- carcinogenic properties. Chemical modification of polysaccharides to increased hydrophobicity and increase functionality has shown great promise in drug delivery systems. Particularly in amorphous solid dispersion (ASD) formulations, hydrophobicity increases miscibility with hydrophobic, crystalline drugs and carboxy functionality provides stabilization with drug moieties and well as pH specific release. Successful synthesis of cellulose ω-carboxyalkanoates have been reported and showed great promise as ASD polymers based on their ability to retard the recrystallization of the HIV drug ritonavir and antibacterial clarithromycin. However, these cellulose derivatives have limitations due to their limited water solubility. Natural pullulan is water-soluble and modification with ω-carboxyalkanoate groups would provide a unique set of derivatives with increased solubility therefore stronger polymer-drug interactions in solution. We have successfully prepared novel pullulan ω-carboxyalkanoates, which exhibit good solubility in polar aprotic and polar protic solvents. -
Biological Stains & Dyes
BIOLOGICAL STAINS & DYES Developed for Biology, microbiology & industrial applications ACRIFLAVIN ALCIAN BLUE 8GX ACRIDINE ORANGE ALIZARINE CYANINE GREEN ANILINE BLUE (SPIRIT SOLUBLE) www.lobachemie.com BIOLOGICAL STAINS & DYES Staining is an important technique used in microscopy to enhance contrast in the microscopic image. Stains and dyes are frequently used in biology and medicine to highlight structures in biological tissues. Loba Chemie offers comprehensive range of Stains and dyes, which are frequently used in Microbiology, Hematology, Histology, Cytology, Protein and DNA Staining after Electrophoresis and Fluorescence Microscopy etc. Many of our stains and dyes have specifications complying certified grade of Biological Stain Commission, and suitable for biological research. Stringent testing on all batches is performed to ensure consistency and satisfy necessary specification particularly in challenging work such as histology and molecular biology. Stains and dyes offer by Loba chemie includes Dry – powder form Stains and dyes as well as wet - ready to use solutions. Features: • Ideally suited to molecular biology or microbiology applications • Available in a wide range of innovative chemical packaging options. Range of Biological Stains & Dyes Product Code Product Name C.I. No CAS No 00590 ACRIDINE ORANGE 46005 10127-02-3 00600 ACRIFLAVIN 46000 8063-24-9 00830 ALCIAN BLUE 8GX 74240 33864-99-2 00840 ALIZARINE AR 58000 72-48-0 00852 ALIZARINE CYANINE GREEN 61570 4403-90-1 00980 AMARANTH 16185 915-67-3 01010 AMIDO BLACK 10B 20470