Western Blot Sandwich ELISA Immunohistochemistry
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Deletion of the Gene Encoding the Reductase Component of 3
Yeh et al. Microbial Cell Factories 2014, 13:130 http://www.microbialcellfactories.com/content/13/1/130 RESEARCH Open Access Deletion of the gene encoding the reductase component of 3-ketosteroid 9α-hydroxylase in Rhodococcus equi USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione Chin-Hsing Yeh1, Yung-Shun Kuo1, Che-Ming Chang1, Wen-Hsiung Liu2, Meei-Ling Sheu3 and Menghsiao Meng1* Abstract The gene encoding the putative reductase component (KshB) of 3-ketosteroid 9α-hydroxylase was cloned from Rhodococcus equi USA-18, a cholesterol oxidase-producing strain formerly named Arthrobacter simplex USA-18, by PCR according to consensus amino acid motifs of several bacterial KshB subunits. Deletion of the gene in R. equi USA-18 by a PCR-targeted gene disruption method resulted in a mutant strain that could accumulate up to 0.58 mg/ml 1,4-androstadiene-3,17-dione (ADD) in the culture medium when 0.2% cholesterol was used as the carbon source, indicating the involvement of the deleted enzyme in 9α-hydroxylation of steroids. In addition, this mutant also accumulated 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid (Δ1,4-BNC). Because both ADD and Δ1,4-BNC are important intermediates for the synthesis of steroid drugs, this mutant derived from R. equi USA-18 may deserve further investigation for its application potential. Background generally believed to be carried out by cholesterol oxidase, Steroid drugs, including androgens, anabolic steroids, es- which catalyzes the oxidation of the 3β-hydroxyl moiety of trogens and corticosteroids, have been widely used for a sterols with the simultaneous isomerization of Δ5 to Δ4, variety of health purposes. -
FANCL Sirna (H): Sc-45661
SAN TA C RUZ BI OTEC HNOL OG Y, INC . FANCL siRNA (h): sc-45661 BACKGROUND STORAGE AND RESUSPENSION Defects in FANCL are a cause of Fanconi anemia. Fanconi anemia (FA) is an Store lyophilized siRNA duplex at -20° C with desiccant. Stable for at least autosomal recessive disorder characterized by bone marrow failure, birth one year from the date of shipment. Once resuspended, store at -20° C, defects and chromosomal instability. At the cellular level, FA is characterized avoid contact with RNAses and repeated freeze thaw cycles. by spontaneous chromosomal breakage and a unique hypersensitivity to DNA Resuspend lyophilized siRNA duplex in 330 µl of the RNAse-free water cross-linking agents. At least 8 complementation groups have been identified pro vided. Resuspension of the siRNA duplex in 330 µl of RNAse-free water and 6 FA genes (for subtypes A, C, D2, E, F and G) have been cloned. Phospho- makes a 10 µM solution in a 10 µM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM rylation of FANC (Fanconi anemia complementation group) proteins is thought EDTA buffered solution. to be important for the function of the FA pathway. FA proteins cooperate in a common pathway, culminating in the monoubiquitination of FANCD2 protein APPLICATIONS and colocalization of FANCD2 and BRCA1 proteins in nuclear foci. FANCL is a ligase protein mediating the ubiquitination of FANCD2, a key step in the FANCL shRNA (h) Lentiviral Particles is recommended for the inhibition of DNA damage pathway. FANCL may be required for proper primordial germ cell FANCL expression in human cells. -
Further Insights Into the Regulation of the Fanconi Anemia FANCD2 Protein
University of Rhode Island DigitalCommons@URI Open Access Dissertations 2015 Further Insights Into the Regulation of the Fanconi Anemia FANCD2 Protein Rebecca Anne Boisvert University of Rhode Island, [email protected] Follow this and additional works at: https://digitalcommons.uri.edu/oa_diss Recommended Citation Boisvert, Rebecca Anne, "Further Insights Into the Regulation of the Fanconi Anemia FANCD2 Protein" (2015). Open Access Dissertations. Paper 397. https://digitalcommons.uri.edu/oa_diss/397 This Dissertation is brought to you for free and open access by DigitalCommons@URI. It has been accepted for inclusion in Open Access Dissertations by an authorized administrator of DigitalCommons@URI. For more information, please contact [email protected]. FURTHER INSIGHTS INTO THE REGULATION OF THE FANCONI ANEMIA FANCD2 PROTEIN BY REBECCA ANNE BOISVERT A DISSERTATION SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY IN CELL AND MOLECULAR BIOLOGY UNIVERSITY OF RHODE ISLAND 2015 DOCTOR OF PHILOSOPHY DISSERTATION OF REBECCA ANNE BOISVERT APPROVED: Dissertation Committee: Major Professor Niall Howlett Paul Cohen Becky Sartini Nasser H. Zawia DEAN OF THE GRADUATE SCHOOL UNIVERSITY OF RHODE ISLAND 2015 ABSTRACT Fanconi anemia (FA) is a rare autosomal and X-linked recessive disorder, characterized by congenital abnormalities, pediatric bone marrow failure and cancer susceptibility. FA is caused by biallelic mutations in any one of 16 genes. The FA proteins function cooperatively in the FA-BRCA pathway to repair DNA interstrand crosslinks (ICLs). The monoubiquitination of FANCD2 and FANCI is a central step in the activation of the FA-BRCA pathway and is required for targeting these proteins to chromatin. -
W W W .Bio Visio N .Co M New Products Added in 2020
New products added in 2020 Please find below a list of all the products added to our portfolio in the year 2020. Assay Kits Product Name Cat. No. Size Product Name Cat. No. Size N-Acetylcysteine Assay Kit (F) K2044 100 assays Human GAPDH Activity Assay Kit II K2047 100 assays Adeno-Associated Virus qPCR Quantification Kit K1473 100 Rxns Human GAPDH Inhibitor Screening Kit (C) K2043 100 assays 20 Preps, Adenovirus Purification Kit K1459 Hydroxyurea Colorimetric Assay Kit K2046 100 assays 100 Preps Iodide Colorimetric Assay Kit K2037 100 assays Aldehyde Dehydrogenase 2 Inhibitor Screening Kit (F) K2011 100 assays Laccase Activity Assay Kit (C) K2038 100 assays Aldehyde Dehydrogenase 3A1 Inhibitor Screening Kit (F) K2060 100 assays 20 Preps, Lentivirus and Retrovirus Purification Kit K1458 Alkaline Phosphatase Staining Kit K2035 50 assays 100 Preps Alpha-Mannosidase Activity Assay Kit (F) K2041 100 assays Instant Lentivirus Detection Card K1470 10 tests, 20 tests Beta-Mannosidase Activity Assay Kit (F) K2045 100 assays Lentivirus qPCR Quantification Kit K1471 100 Rxns 50 Preps, Buccal Swab DNA Purification Kit K1466 Maleimide Activated KLH-Peptide Conjugation Kit K2039 5 columns 250 Preps Methionine Adenosyltransferase Activity Assay Kit (C) K2033 100 assays CD38 Activity Assay Kit (F) K2042 100 assays miRNA Extraction Kit K1456 50 Preps EZCell™ CFDA SE Cell Tracer Kit K2057 200 assays MMP-13 Inhibitor Screening Kit (F) K2067 100 assays Choline Oxidase Activity Assay Kit (F) K2052 100 assays Mycoplasma PCR Detection Kit K1476 100 Rxns Coronavirus -
At Elevated Temperatures, Heat Shock Protein Genes Show Altered Ratios Of
EXPERIMENTAL AND THERAPEUTIC MEDICINE 22: 900, 2021 At elevated temperatures, heat shock protein genes show altered ratios of different RNAs and expression of new RNAs, including several novel HSPB1 mRNAs encoding HSP27 protein isoforms XIA GAO1,2, KEYIN ZHANG1,2, HAIYAN ZHOU3, LUCAS ZELLMER4, CHENGFU YUAN5, HAI HUANG6 and DEZHONG JOSHUA LIAO2,6 1Department of Pathology, Guizhou Medical University Hospital; 2Key Lab of Endemic and Ethnic Diseases of The Ministry of Education of China in Guizhou Medical University; 3Clinical Research Center, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China; 4Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA; 5Department of Biochemistry, China Three Gorges University, Yichang, Hubei 443002; 6Center for Clinical Laboratories, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China Received December 16, 2020; Accepted May 10, 2021 DOI: 10.3892/etm.2021.10332 Abstract. Heat shock proteins (HSP) serve as chaperones genes may engender multiple protein isoforms. These results to maintain the physiological conformation and function of collectively suggested that, besides increasing their expres‑ numerous cellular proteins when the ambient temperature is sion, certain HSP and associated genes also use alternative increased. To determine how accurate the general assumption transcription start sites to produce multiple RNA transcripts that HSP gene expression is increased in febrile situations is, and use alternative splicing of a transcript to produce multiple the RNA levels of the HSF1 (heat shock transcription factor 1) mature RNAs, as important mechanisms for responding to an gene and certain HSP genes were determined in three cell increased ambient temperature in vitro. lines cultured at 37˚C or 39˚C for three days. -
The Comparative Enzymology and Cell Origin of Rat Hepatomas II
The Comparative Enzymology and Cell Origin of Rat Hepatomas II. Glutamate Dehydrogenase, Choline Oxidase, and Glucose-6-phosphatase* HENRY C. PITOT~ (McArdle Memorial Laboratory, The Medical School, University of Wisconsin, Madison, Wis.) SUMMARY The activities of glucose-6-phosphatase, glutamate dehydrogcnase, and choline ox[- dase were determined in some or all of ten rat hepatomas, including the Novikoff, Dunning L-C18, McCoy MDAB, and the Morris 3683, 39524A, and 51~3 hepatomas, together with primary hepatomas produced by feeding ethionine or 3%nethyl-4- dimethylaminoazobenzene, and transplanted hepatomas derived from the primary tumors induced with ethionine. Of these neoplasms, only the Morris hepatoma 51~3, the primary and transplanted ethionine-induced hepatomas, and one of the 3'-methyl-4-dimethylaminoazobenzene- induced tumors possessed significant glucose-6-phosphatase activity. These same tu- mors in addition to the Dunning L-C18 hepatoma had demonstrable glutamate dehydro- genase activity, whereas the other neoplasms tested failed to show significant activity of this enzyme. With the exception of the primary dye-induced neoplasm, which was not tested, only those neoplasms having significant glucose-6-phosphatase activities showed any choline oxidase activity. Of those neoplasms tested for tryptophan peroxidase activity only the Morris hepa- toma 51~3, the primary ethionine-induced hepatoma, and some of the Dunning L-C18 hepatomas had any demonstrable activity of this enzyme. In contrast to most of the enzymatic activities reported here, the threonine dehydrase activity of the Morris hepatoma 51r was of the order of 40 times the level of this enzyme in the livers of animals bearing this tumor. -
The PI3K/Akt1 Pathway Enhances Steady-State Levels of FANCL
This is a repository copy of The PI3K/Akt1 pathway enhances steady-state levels of FANCL. White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/153365/ Version: Published Version Article: Dao, K.-H.T., Rotelli, M.D., Brown, B.R. et al. (6 more authors) (2013) The PI3K/Akt1 pathway enhances steady-state levels of FANCL. Molecular Biology of the Cell, 24 (16). pp. 2582-2592. https://doi.org/10.1091/mbc.E13-03-0144 Reuse This article is distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike (CC BY-NC-SA) licence. This licence allows you to remix, tweak, and build upon this work non-commercially, as long as you credit the authors and license your new creations under the identical terms. More information and the full terms of the licence here: https://creativecommons.org/licenses/ Takedown If you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing [email protected] including the URL of the record and the reason for the withdrawal request. [email protected] https://eprints.whiterose.ac.uk/ M BoC | ARTICLE The PI3K/Akt1 pathway enhances steady-state levels of FANCL Kim-Hien T. Daoa, Michael D. Rotellia, Brieanna R. Browna, Jane E. Yatesa,b, Juha Rantalac, Cristina Tognona, Jeffrey W. Tynera,d, Brian J. Drukera,e,*, and Grover C. Bagbya,b,* aKnight Cancer Institute, cDepartment of Biomedical Engineering, dDepartment of Cell and Developmental Biology, and eHoward Hughes Medical Institute, Oregon Health and Science University, Portland, OR 97239; bNorthwest VA Cancer Research Center, VA Medical Center Portland, Portland, OR 97239 ABSTRACT Fanconi anemia hematopoietic stem cells display poor self-renewal capacity Monitoring Editor when subjected to a variety of cellular stress. -
Production of 4-Ene-3-Ketosteroids in Corynebacterium Glutamicum
catalysts Article Production of 4-Ene-3-ketosteroids in Corynebacterium glutamicum Julia García-Fernández 1, Beatriz Galán 1, Carmen Felpeto-Santero 1, José L. Barredo 2 and José L. García 1,* 1 Department of Environmental Biotechnology, Centro de Investigaciones Biológicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain; [email protected] (J.G.-F.); [email protected] (B.G.); [email protected] (C.F.-S.) 2 Department of Biotechnology, Crystal Pharma, A Division of Albany Molecular Research Inc. (AMRI), 47151 Boecillo Valladolid, Spain; [email protected] * Correspondence: [email protected]; Tel.: +34-918-373-112 Received: 29 September 2017; Accepted: 20 October 2017; Published: 27 October 2017 Abstract: Corynebacterium glutamicum has been widely used for the industrial production of amino acids and many value-added chemicals; however, it has not been exploited for the production of steroids. Using C. glutamicum as a cellular biocatalyst we have expressed the 3β-hydroxysteroid dehydrogenase/isomerase MSMEG_5228 from Mycobacterium smegmatis to demonstrate that the resulting recombinant strain is able to oxidize in vivo C19 and C21 3-OH-steroids to their corresponding keto-derivatives. This new approach constitutes a proof of concept of a biotechnological process for producing value-added intermediates such as 4-pregnen-16α,17α-epoxy-16β-methyl-3,20-dione. Keywords: 3-OH-steroids; biotransformation; dehydrogenase; Rhodococcus and Corynebacterium expression systems 1. Introduction Corynebacterium glutamicum has been widely used for the industrial production of amino acids, but the publication of its complete genome [1,2] has provided the basis for an enormous progress in the use of this microorganism for other biotechnological applications placing it as an ideal chassis within the top ranking of cell factories [3]. -
Table S2.Up Or Down Regulated Genes in Tcof1 Knockdown Neuroblastoma N1E-115 Cells Involved in Differentbiological Process Anal
Table S2.Up or down regulated genes in Tcof1 knockdown neuroblastoma N1E-115 cells involved in differentbiological process analysed by DAVID database Pop Pop Fold Term PValue Genes Bonferroni Benjamini FDR Hits Total Enrichment GO:0044257~cellular protein catabolic 2.77E-10 MKRN1, PPP2R5C, VPRBP, MYLIP, CDC16, ERLEC1, MKRN2, CUL3, 537 13588 1.944851 8.64E-07 8.64E-07 5.02E-07 process ISG15, ATG7, PSENEN, LOC100046898, CDCA3, ANAPC1, ANAPC2, ANAPC5, SOCS3, ENC1, SOCS4, ASB8, DCUN1D1, PSMA6, SIAH1A, TRIM32, RNF138, GM12396, RNF20, USP17L5, FBXO11, RAD23B, NEDD8, UBE2V2, RFFL, CDC GO:0051603~proteolysis involved in 4.52E-10 MKRN1, PPP2R5C, VPRBP, MYLIP, CDC16, ERLEC1, MKRN2, CUL3, 534 13588 1.93519 1.41E-06 7.04E-07 8.18E-07 cellular protein catabolic process ISG15, ATG7, PSENEN, LOC100046898, CDCA3, ANAPC1, ANAPC2, ANAPC5, SOCS3, ENC1, SOCS4, ASB8, DCUN1D1, PSMA6, SIAH1A, TRIM32, RNF138, GM12396, RNF20, USP17L5, FBXO11, RAD23B, NEDD8, UBE2V2, RFFL, CDC GO:0044265~cellular macromolecule 6.09E-10 MKRN1, PPP2R5C, VPRBP, MYLIP, CDC16, ERLEC1, MKRN2, CUL3, 609 13588 1.859332 1.90E-06 6.32E-07 1.10E-06 catabolic process ISG15, RBM8A, ATG7, LOC100046898, PSENEN, CDCA3, ANAPC1, ANAPC2, ANAPC5, SOCS3, ENC1, SOCS4, ASB8, DCUN1D1, PSMA6, SIAH1A, TRIM32, RNF138, GM12396, RNF20, XRN2, USP17L5, FBXO11, RAD23B, UBE2V2, NED GO:0030163~protein catabolic process 1.81E-09 MKRN1, PPP2R5C, VPRBP, MYLIP, CDC16, ERLEC1, MKRN2, CUL3, 556 13588 1.87839 5.64E-06 1.41E-06 3.27E-06 ISG15, ATG7, PSENEN, LOC100046898, CDCA3, ANAPC1, ANAPC2, ANAPC5, SOCS3, ENC1, SOCS4, -
Insight V-CHEM General Health Profile
【Product Name】 General Health Profile 【Packing Specification】 1 Disc / Sample 【Instrument】 See the InSight V-CHEM chemistry analyser Operator’s Manual for complete information on use of the analyser. 【Intended Use】 The General Health Profile used with the InSight V-CHEM chemistry analyser is intended to be used for the in vitro quantitative determination of total Protein (TP), albumin (ALB), total bilirubin (TBIL), alanine aminotransferase (ALT), blood urea (BUN), creatinine (CRE), amylase (AMY), creatinekinase (CK), calcium (Ca2+), phosphorus (P), alkaline Phosphatase (ALP), glucose (GLU), and total cholesterol (CHOL)in heparinised whole blood, heparinised plasma, or serum in a clinical laboratory setting or point of care location. The General Health Profile and the InSight V-CHEM chemistry analyser comprise an in vitro diagnostic system that aids the physician in the following disorders: liver and gall bladder diseases, urinary system diseases, carbohydrate metabolism disorders, lipid metabolism disorders, cardiovascular disease and pancreatic diseases. 【Test Principles】 This product, which is based on spectrophotometry, is used to quantitatively determine the concentration or activity of the 13 biochemical indicators in the sample. The test principles are as follows: (1) Total Protein (TP) The total protein method is a Biuret reaction, the protein solution is treated with cupric [Cu(II)] ions in a strong alkaline medium. The Cu(II) ions react with peptide bonds between the carbonyl oxygen and amide nitrogen atoms to form a coloured Cu-protein complex. The amount of total protein present in the sample is directly proportional to the absorbance of the Cu-protein complex. The total protein test is an endpoint reaction and the absorbance is measured as the difference in absorbance between 550 nm and 800 nm. -
A Review on Glucose Oxidase
Int.J.Curr.Microbiol.App.Sci (2015) 4(8): 636-642 International Journal of Current Microbiology and Applied Sciences ISSN: 2319-7706 Volume 4 Number 8 (2015) pp. 636-642 http://www.ijcmas.com Review Article A Review on Glucose Oxidase Shaikh Sumaiya A* and Ratna Trivedi Department of Microbiology, Shree Ramkrishna Institute of Applied Sciences, Athwalines, Surat-395001, India *Corresponding author ABSTRACT K eywo rd s Glucose oxidase (GOX) from Aspergillus niger is a very much portrayed glycoprotein comprising of two indistinguishable 80-kDa subunits with two Glucose oxidase FAD co-factors bound. Both the DNA grouping and protein structure at 1.9 (GOX; GOD), Ǻ have been resolved. GOX catalyzes the oxidation of D- glucose (C6H12O6) Food to D-gluconolactone (C H O ) and hydrogen peroxide. GOX production is processing, 6 10 6 natural in some fungi and insects where its reactant by-product, hydrogen Additive, peroxide, goes about as a hostile to bacterial and against fungal cultures. Enzyme , Properties , GOX is Generally Regarded as Safe (GRAS), and GOX from A. niger is the Physical premise of numerous modern applications. GOX-catalyzed response uproots properties , oxygen and produces hydrogen peroxide, a characteristic used in Structure, nourishment protection. This paper will give a brief foundation on the Stability , normal event, capacities, weaknesses of different chemicals that oxidize Substrates, glucose, Isolation of and early deal with the protein, structure of GOD and Reaction how it identifies with the immobiliz ation and strength of the chemical and in mechanism addition the properties of glucose oxidase. Introduction The living cell is the site of huge This building up and tearing down happens biochemical movement called metabolism. -
Inactivation of Choline Oxidase by Irreversible Inhibitors Or Storage Conditions
Georgia State University ScholarWorks @ Georgia State University Chemistry Theses Department of Chemistry 8-3-2006 Inactivation of Choline Oxidase by Irreversible Inhibitors or Storage Conditions Jane Vu Hoang [email protected] Follow this and additional works at: https://scholarworks.gsu.edu/chemistry_theses Recommended Citation Hoang, Jane Vu, "Inactivation of Choline Oxidase by Irreversible Inhibitors or Storage Conditions." Thesis, Georgia State University, 2006. https://scholarworks.gsu.edu/chemistry_theses/4 This Thesis is brought to you for free and open access by the Department of Chemistry at ScholarWorks @ Georgia State University. It has been accepted for inclusion in Chemistry Theses by an authorized administrator of ScholarWorks @ Georgia State University. For more information, please contact [email protected]. INACTIVATION OF CHOLINE OXIDASE BY IRREVERSIBLE INHIBITORS OR STORAGE CONDITIONS by JANE V. HOANG Under the Direction of Giovanni Gadda ABSTRACT Choline oxidase from Arthrobacter globiformis is a flavin-dependent enzyme that catalyzes the oxidation of choline to betaine aldehyde through two sequential hydride-transfer steps. The study of this enzyme is of importance to the understanding of glycine betaine biosynthesis found in pathogenic bacterial or economic relevant crop plants as a response to temperature and salt stress in adverse environment. In this study, chemical modification of choline oxidase using two irreversible inhibitors, tetranitromethane and phenylhydrazine, was performed in order to gain insights into the active site structure of the enzyme. Choline oxidase can also be inactivated irreversibly by freezing in 20 mM sodium phosphate and 20 mM sodium pyrophosphate at pH 6 and -20 oC. The results showed that enzyme inactivation was due to a localized conformational change associated with the ionization of a group in close proximity to the flavin cofactor and led to a complete lost of catalytic activity.