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Produktinformation Diagnostik & molekulare Diagnostik Laborgeräte & Service Zellkultur & Verbrauchsmaterial Forschungsprodukte & Biochemikalien Weitere Information auf den folgenden Seiten! See the following pages for more information! Lieferung & Zahlungsart Lieferung: frei Haus Bestellung auf Rechnung SZABO-SCANDIC Lieferung: € 10,- HandelsgmbH & Co KG Erstbestellung Vorauskassa Quellenstraße 110, A-1100 Wien T. +43(0)1 489 3961-0 Zuschläge F. +43(0)1 489 3961-7 [email protected] • Mindermengenzuschlag www.szabo-scandic.com • Trockeneiszuschlag • Gefahrgutzuschlag linkedin.com/company/szaboscandic • Expressversand facebook.com/szaboscandic Tel:240-252-7368(USA) Fax:240-252-7376(USA) www.elabscience.com ® E-mail:[email protected] Elabscience Elabscience Biotechnology Inc. TMPRSS11D Polyclonal Antibody Catalog No. E-AB-17120 Reactivity H Storage Store at -20℃. Avoid freeze / thaw cycles. Host Rabbit Applications WB,IHC,ELISA ElabscienceIsotype IgG Note: Centrifuge before opening to ensure complete recovery of vial contents. Images Immunogen Information Elabscience Immunogen Fusion protein of human TMPRSS11D Gene Accession BC125195 Swissprot O60235 Synonyms Ac2-223,asd,Beta G1,Beta glucuronidase,Beta-G1,Bet a-glucuronidase,BG,BGLR,FLJ39445,Glucuronidase beta,Gur,Gus,Gus-r,Gus-s,Gus-t,Gus- u,GUSB,Gut,MPS7 Immunohistochemistry of paraffin- Product Information embedded Human liver cancer using Calculated MW 46 kDa TMPRSS11D Polyclonal Antibody at Buffer PBS with 0.05% sodium azide and 50% glycerol, dilution of 1/35 PH7.4 Purify Affinity purification Dilution WB 1:500-2000, IHC 1:25-100, ELISA 1:2000-5000 Elabscience Background This gene encodes a trypsin-like serine protease released from the submucosal serous glands onto mucous membrane. It is a type II integral Western Blot analysis of Human thigh membrane protein and has 29-38% identity in the sequence of the malignant fibrous histiocytoma tissue catalytic region with human hepsin, enteropeptidase, acrosin, and mast using TMPRSS11D Polyclonal cell tryptase. The noncatalytic region has little similarity to other known Antibody at dilution of 1/800 proteins.Elabscience Elabscience For Research Use Only Focus on your research Thank you for your recent purchase. If you would like to learn more about antibodies,please visit www.elabscience.com. Service for life science Applications:WB-Western Blot IHC-Immunohistochemistry IF-Immunofluorescence IP-Immunoprecipitation FC-Flow cytometry ChIP- Chromatin Immunoprecipitation Reactivity: H-HumanElabscience R-Rat M-Mouse Mk-Monkey Dg-Dog Ch-Chicken Hm-Hamster Rb-Rabbit Sh- Sheep Pg-Pig Z-Zebrafish X-Xenopus C-Cow. Powered by TCPDF (www.tcpdf.org).

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Congenital Diarrheal Disorders: an Updated Diagnostic Approach
4168 Int. J. Mol. Sci.2012, 13, 4168-4185; doi:10.3390/ijms13044168 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Review Congenital Diarrheal Disorders: An Updated Diagnostic Approach Gianluca Terrin 1, Rossella Tomaiuolo 2,3,4, Annalisa Passariello 5, Ausilia Elce 2,3, Felice Amato 2,3, Margherita Di Costanzo 5, Giuseppe Castaldo 2,3 and Roberto Berni Canani 5,6,* 1 Department of Gynecology-Obstetrics and Perinatal Medicine, University of Rome “La Sapienza”, Viale del Policlinico 1, Rome 00161, Italy; E-Mail: [email protected] 2 CEINGE-Advanced Biotechnology, Via Comunale Margherita, Naples 80131, Italy; E-Mails: [email protected] (R.T.); [email protected] (A.E.); [email protected] (F.A.); [email protected] (G.C.) 3 Department of Biochemistry and Biotechnology, University of Naples “Federico II”, Via Pansini 5, Naples 80131, Italy 4 Biotechnology Science, University of Naples “Federico II”, Via De Amicis, Naples 80131, Italy 5 Department of Pediatrics, University of Naples “Federico II”, Via Pansini 5, Naples 80131, Italy; E-Mails: [email protected] (A.P.); [email protected] (M.D.C.) 6 European Laboratory for the Investigation of Food Induced Diseases, University of Naples “Federico II”, Via Pansini 5, Naples 80131, Italy * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel./Fax: +39-0817462680. Received: 18 February 2012; in revised form: 2 March 2012 / Accepted: 19 March 2012 / Published: 29 March 2012 Abstract: Congenital diarrheal disorders (CDDs) are a group of inherited enteropathies with a typical onset early in the life.
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Purification and Identification of a Binding Protein for Pancreatic
Biochem. J. (2003) 372, 227–233 (Printed in Great Britain) 227 Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: a novel role of the inhibitor as an anti-granzyme A Satoshi TSUZUKI*1,2,Yoshimasa KOKADO*1, Shigeki SATOMI*, Yoshie YAMASAKI*, Hirofumi HIRAYASU*, Toshihiko IWANAGA† and Tohru FUSHIKI* *Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan, and †Laboratory of Anatomy, Graduate School of Veterinary Medicine, Hokkaido University, Kita 18-Nishi 9, Kita-ku, Sapporo 060-0818, Japan Pancreatic secretory trypsin inhibitor (PSTI) is a potent trypsin of GzmA-expressing intraepithelial lymphocytes in the rat small inhibitor that is mainly found in pancreatic juice. PSTI has been intestine. We concluded that the PSTI-binding protein isolated shown to bind specifically to a protein, distinct from trypsin, on from the dispersed cells is GzmA that is produced in the the surface of dispersed cells obtained from tissues such as small lymphocytes of the tissue. The rGzmA hydrolysed the N-α- intestine. In the present study, we affinity-purified the binding benzyloxycarbonyl-L-lysine thiobenzyl ester (BLT), and the BLT protein from the 2 % (w/v) Triton X-100-soluble fraction of hydrolysis was inhibited by PSTI. Sulphated glycosaminoglycans, dispersed rat small-intestinal cells using recombinant rat PSTI. such as fucoidan or heparin, showed almost no effect on the Partial N-terminal sequencing of the purified protein gave a inhibition of rGzmA by PSTI, whereas they decreased the inhi- sequence that was identical with the sequence of mouse granzyme bition by antithrombin III.
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Molecular Markers of Serine Protease Evolution
The EMBO Journal Vol. 20 No. 12 pp. 3036±3045, 2001 Molecular markers of serine protease evolution Maxwell M.Krem and Enrico Di Cera1 ment and specialization of the catalytic architecture should correspond to signi®cant evolutionary transitions in the Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St Louis, history of protease clans. Evolutionary markers encoun- MO 63110-1093, USA tered in the sequences contributing to the catalytic apparatus would thus give an account of the history of 1Corresponding author e-mail: [email protected] an enzyme family or clan and provide for comparative analysis with other families and clans. Therefore, the use The evolutionary history of serine proteases can be of sequence markers associated with active site structure accounted for by highly conserved amino acids that generates a model for protease evolution with broad form crucial structural and chemical elements of applicability and potential for extension to other classes of the catalytic apparatus. These residues display non- enzymes. random dichotomies in either amino acid choice or The ®rst report of a sequence marker associated with serine codon usage and serve as discrete markers for active site chemistry was the observation that both AGY tracking changes in the active site environment and and TCN codons were used to encode active site serines in supporting structures. These markers categorize a variety of enzyme families (Brenner, 1988). Since serine proteases of the chymotrypsin-like, subtilisin- AGY®TCN interconversion is an uncommon event, it like and a/b-hydrolase fold clans according to phylo- was reasoned that enzymes within the same family genetic lineages, and indicate the relative ages and utilizing different active site codons belonged to different order of appearance of those lineages.
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University of South Florida Scholar Commons Graduate Theses and Dissertations Graduate School July 2017 Role of Amylase in Ovarian Cancer Mai Mohamed University of South Florida, [email protected] Follow this and additional works at: http://scholarcommons.usf.edu/etd Part of the Pathology Commons Scholar Commons Citation Mohamed, Mai, "Role of Amylase in Ovarian Cancer" (2017). Graduate Theses and Dissertations. http://scholarcommons.usf.edu/etd/6907 This Dissertation is brought to you for free and open access by the Graduate School at Scholar Commons. It has been accepted for inclusion in Graduate Theses and Dissertations by an authorized administrator of Scholar Commons. For more information, please contact [email protected]. Role of Amylase in Ovarian Cancer by Mai Mohamed A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy Department of Pathology and Cell Biology Morsani College of Medicine University of South Florida Major Professor: Patricia Kruk, Ph.D. Paula C. Bickford, Ph.D. Meera Nanjundan, Ph.D. Marzenna Wiranowska, Ph.D. Lauri Wright, Ph.D. Date of Approval: June 29, 2017 Keywords: ovarian cancer, amylase, computational analyses, glycocalyx, cellular invasion Copyright © 2017, Mai Mohamed Dedication This dissertation is dedicated to my parents, Ahmed and Fatma, who have always stressed the importance of education, and, throughout my education, have been my strongest source of encouragement and support. They always believed in me and I am eternally grateful to them. I would also like to thank my brothers, Mohamed and Hussien, and my sister, Mariam. I would also like to thank my husband, Ahmed.
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Cell Surface–Anchored Serine Proteases in Cancer Progression and Metastasis
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Hippo and Sonic Hedgehog Signalling Pathway Modulation of Human Urothelial Tissue Homeostasis
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Isolation and Characterization of Porcine Ott-Proteinase Inhibitor1),2) Leukocyte Elastase-Inhibitor Complexes in Porcine Blood, I
Geiger, Leysath and Fritz: Porcine otrproteinase inhibitor 637 J. Clin. Chem. Clin. Biochem. Vol. 23, 1985, pp. 637-643 Isolation and Characterization of Porcine ott-Proteinase Inhibitor1),2) Leukocyte Elastase-Inhibitor Complexes in Porcine Blood, I. By R. Geiger, Gisela Leysath and H. Fritz Abteilung für Klinische Chemie und Klinische Biochemie (Leitung: Prof. Dr. H. Fritz) in der Chirurgischen Klinik Innenstadt der Universität München (Received March 18/June 20, 1985) Summary: arProteinase inhibitor was purified from procine blood by ammonium sulphate and Cibachron Blue-Sepharose fractionation, ion exchange chromatography on DEAE-Cellulose, gel filtration on Sephadex G-25, and zinc chelating chromatography. Thus, an inhibitor preparation with a specific activity of 1.62 lU/mgprotein (enzyme: trypsin; Substrate: BzArgNan) was obtained. In sodium dodecyl sulphate gel electroph- oresis one protein band corresponding to a molecular mass of 67.6 kDa was found. On isoelectric focusing 6 protein bands with isoelectric points of 3.80, 3.90, 4.05, 4.20, 4.25 and 4.45 were separated. The amino acid composition was determined. The association rate constants for the Inhibition of various serine proteinases were measured. Isolierung und Charakterisierung des on-Proteinaseinhibitors des Schweins Leukocyten-oLj-Proteinaseinhibitor-Komplexe in Schweineblut, L Zusammenfassung; arProteinaseinhibitor wurde aus Schweineblut mittels Ammoniumsulfatfallung und Frak- tionierung an Cibachron-Blau-Sepharose, lonenaustauschchromatographie an DEAE-Cellulose, Gelfiltration an Sephadex G-25 und Zink-Chelat-Chromatographie isoliert. Die erhaltene Inhibitor-Präparation hatte eine spezifische Aktivität von 1,62 ITJ/mg Protein (Enzym: Trypsin; Substrat: BzArgNan). In der Natriumdodecyl- sulfat-Elektrophorese wurde eine Proteinbande mit einer dazugehörigen Molekülmasse von 67,6 kDa erhalten.
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N-Glycosylation in the Protease Domain of Trypsin-Like Serine Proteases Mediates Calnexin-Assisted Protein Folding
RESEARCH ARTICLE N-glycosylation in the protease domain of trypsin-like serine proteases mediates calnexin-assisted protein folding Hao Wang1,2, Shuo Li1, Juejin Wang1†, Shenghan Chen1‡, Xue-Long Sun1,2,3,4, Qingyu Wu1,2,5* 1Molecular Cardiology, Cleveland Clinic, Cleveland, United States; 2Department of Chemistry, Cleveland State University, Cleveland, United States; 3Chemical and Biomedical Engineering, Cleveland State University, Cleveland, United States; 4Center for Gene Regulation of Health and Disease, Cleveland State University, Cleveland, United States; 5Cyrus Tang Hematology Center, State Key Laboratory of Radiation Medicine and Prevention, Soochow University, Suzhou, China Abstract Trypsin-like serine proteases are essential in physiological processes. Studies have shown that N-glycans are important for serine protease expression and secretion, but the underlying mechanisms are poorly understood. Here, we report a common mechanism of N-glycosylation in the protease domains of corin, enteropeptidase and prothrombin in calnexin- mediated glycoprotein folding and extracellular expression. This mechanism, which is independent *For correspondence: of calreticulin and operates in a domain-autonomous manner, involves two steps: direct calnexin [email protected] binding to target proteins and subsequent calnexin binding to monoglucosylated N-glycans. Elimination of N-glycosylation sites in the protease domains of corin, enteropeptidase and Present address: †Department prothrombin inhibits corin and enteropeptidase cell surface expression and prothrombin secretion of Physiology, Nanjing Medical in transfected HEK293 cells. Similarly, knocking down calnexin expression in cultured University, Nanjing, China; ‡Human Aging Research cardiomyocytes and hepatocytes reduced corin cell surface expression and prothrombin secretion, Institute, School of Life Sciences, respectively. Our results suggest that this may be a general mechanism in the trypsin-like serine Nanchang University, Nanchang, proteases with N-glycosylation sites in their protease domains.
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Chymotrypsin C (Caldecrin) Promotes Degradation of Human Cationic Trypsin: Identity with Rinderknecht’S Enzyme Y
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