Quantikine® ELISA

Total Page:16

File Type:pdf, Size:1020Kb

Quantikine® ELISA Quantikine® ELISA Human ADAMTS13 Immunoassay Catalog Number DADT130 For the quantitative determination of human A Disintegrin And Metalloproteinase with Thombospondin type 1 motif, 13 (ADAMTS13) concentrations in cell culture supernates, serum, and plasma. This package insert must be read in its entirety before using this product. For research use only. Not for use in diagnostic procedures. TABLE OF CONTENTS SECTION PAGE INTRODUCTION .....................................................................................................................................................................1 PRINCIPLE OF THE ASSAY ...................................................................................................................................................2 LIMITATIONS OF THE PROCEDURE .................................................................................................................................2 TECHNICAL HINTS .................................................................................................................................................................2 MATERIALS PROVIDED & STORAGE CONDITIONS ...................................................................................................3 OTHER SUPPLIES REQUIRED .............................................................................................................................................4 PRECAUTIONS .........................................................................................................................................................................4 SAMPLE COLLECTION & STORAGE .................................................................................................................................4 SAMPLE PREPARATION........................................................................................................................................................4 REAGENT PREPARATION .....................................................................................................................................................5 ASSAY PROCEDURE .............................................................................................................................................................6 CALCULATION OF RESULTS ...............................................................................................................................................7 TYPICAL DATA .........................................................................................................................................................................7 PRECISION ................................................................................................................................................................................8 RECOVERY.................................................................................................................................................................................8 LINEARITY .................................................................................................................................................................................9 SENSITIVITY .............................................................................................................................................................................9 CALIBRATION ..........................................................................................................................................................................9 SAMPLE VALUES .....................................................................................................................................................................9 SPECIFICITY ........................................................................................................................................................................... 10 REFERENCES ......................................................................................................................................................................... 10 Manufactured and Distributed by: USA R&D Systems, Inc. 614 McKinley Place NE, Minneapolis, MN 55413 TEL: 800 343 7475 612 379 2956 FAX: 612 656 4400 E-MAIL: [email protected] Distributed by: Europe | Middle East | Africa Bio-Techne Ltd. China Bio-Techne China Co., Ltd. 19 Barton Lane, Abingdon Science Park Unit 1901, Tower 3, Raffles City Changning Office, Abingdon OX14 3NB, UK 1193 Changning Road, Shanghai PRC 200051 TEL: +44 (0)1235 529449 TEL: +86 (21) 52380373 (400) 821-3475 FAX: +44 (0)1235 533420 FAX: +86 (21) 52371001 E-MAIL: [email protected] E-MAIL: [email protected] INTRODUCTION ADAMTS13 (A Disintegrin And Metalloproteinase with Thrombospondin type 1 motif, 13), also known as von Willebrand factor (vWF)-cleaving protease, belongs to the ADAMTS superfamily of secreted multidomain zinc metalloproteases. Full-length human ADAMTS13 contains 1427 amino acid residues that are organized into the following domains: signal peptide, propeptide, catalytic, disintegrin-like, thrombospondin type 1 (TSP1), cysteine rich, spacer, seven TSP1 repeats, and two CUB domains. The propeptide contains a furin cleavage consensus motif and is most likely removed in the Golgi or at the cell surface, releasing the 190 kDa active enzyme (1-4). ADAMTS13 is mainly produced by the liver and circulates in the blood (5). vWF, the only known substrate for ADAMTS13, is a large multimeric glycoprotein that is required for platelet adhesion and thrombus formation (1, 2, 6). The hemostatic potential of vWF increases with its length. ADAMTS13 cleaves the ultra-large multimeric vWF (ULvWF) within the A2 domain between Tyr1605 and Met1606, generating smaller, less adhesive multimers (1, 7). Shear stress is required to induce a conformational change in the ULvWF fibers to expose the cleavage site (8). In addition to its role in platelet adhesion, ULvWF has been shown to promote leukocyte adhesion and extravasation during inflammation (9). By cleaving ULvWF, ADAMTS13 down-regulates not only thrombosis but also inflammation. As a result, decreased ADAMTS13 activity accelerates inflammatory diseases and is associated with acute and chronic inflammation (9, 10). ADAMTS13 deficiency as a result of hereditary gene mutations or inhibitory autoantibodies to ADAMTS13 is a cause of thrombotic thrombocytopenic purpura (TTP), which is a rare condition of the blood-coagulation system. TTP is characterized by extensive formation of microthrombi in the microvasculature and may be accompanied by neurological dysfunction and renal failure (11-15). Additional pathologies associated with decreased circulating ADAMTS13 include liver cirrhosis, sepsis, alcoholic hepatitis, and acute pancreatitis (16-19). Low plasma ADAMTS13 is a useful predictor of cardiac and cerebrovascular events in coronary artery diseases (20, 21). After acute myocardial infarction, early decrease of ADAMTS13 levels is a predictor of future thrombotic events (22). In atrial fibrillation (AF), ADAMTS13 level in patients after treatment with cardioconversion is useful for prediction of recurrence of AF (23). The Quantikine® Human ADAMTS13 Immunoassay is a 4.5 hour solid-phase ELISA designed to measure human ADAMTS13 in cell culture supernates, serum, and plasma. It contains CHO cell-expressed recombinant human ADAMTS13 and has been shown to accurately quantitate the recombinant factor. Results obtained using natural human ADAMTS13 showed linear curves that were parallel to the standard curves obtained using the Quantikine® kit standards. These results indicate that this kit can be used to determine relative mass values for natural human ADAMTS13. www.RnDSystems.com 1 PRINCIPLE OF THE ASSAY This assay employs the quantitative sandwich enzyme immunoassay technique. A monoclonal antibody specific for human ADAMTS13 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any ADAMTS13 present is bound by the immobilized antibody. After washing away any unbound substances, an enzyme-linked polyclonal antibody specific for human ADAMTS13 is added to the wells. Following a wash to remove any unbound antibody-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of ADAMTS13 bound in the initial step. The color development is stopped and the intensity of the color is measured. LIMITATIONS OF THE PROCEDURE • FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES. • The kit should not be used beyond the expiration date on the kit label. • Do not mix or substitute reagents with those from other lots or sources. • If samples generate values higher than the highest standard, further dilute the samples with calibrator diluent and repeat the assay. • Any variation in diluent, operator, pipetting technique, washing technique, incubation time or temperature, and kit age can cause variation in binding. • This assay is designed to eliminate interference by other factors present in biological samples. Until these factors have been tested in the Quantikine® Immunoassay, the possibility of interference cannot be excluded. TECHNICAL HINTS • When mixing or reconstituting protein solutions, always avoid foaming. • To avoid cross-contamination, change pipette tips between additions of each standard level, between sample additions, and between reagent additions. Also, use separate reservoirs for each reagent. • To ensure accurate results, proper adhesion of plate sealers during incubation
Recommended publications
  • What Are the Roles of Metalloproteinases in Cartilage and Bone Damage? G Murphy, M H Lee
    iv44 Ann Rheum Dis: first published as 10.1136/ard.2005.042465 on 20 October 2005. Downloaded from REPORT What are the roles of metalloproteinases in cartilage and bone damage? G Murphy, M H Lee ............................................................................................................................... Ann Rheum Dis 2005;64:iv44–iv47. doi: 10.1136/ard.2005.042465 enzyme moiety into an upper and a lower subdomain. A A role for metalloproteinases in the pathological destruction common five stranded beta-sheet and two alpha-helices are in diseases such as rheumatoid arthritis and osteoarthritis, always found in the upper subdomain with a further C- and the irreversible nature of the ensuing cartilage and bone terminal helix in the lower subdomain. The catalytic sites of damage, have been the focus of much investigation for the metalloproteinases, especially the MMPs, have been several decades. This has led to the development of broad targeted for the development of low molecular weight spectrum metalloproteinase inhibitors as potential therapeu- synthetic inhibitors with a zinc chelating moiety. Inhibitors tics. More recently it has been appreciated that several able to fully differentiate between individual enzymes have families of zinc dependent proteinases play significant and not been identified thus far, although a reasonable level of varied roles in the biology of the resident cells in these tissues, discrimination is now being achieved in some cases.7 Each orchestrating development, remodelling, and subsequent family does, however, have other unique domains with pathological processes. They also play key roles in the numerous roles, including the determination of physiological activity of inflammatory cells. The task of elucidating the substrate specificity, ECM, or cell surface localisation (fig 1).
    [Show full text]
  • And MMP-Mediated Cell–Matrix Interactions in the Tumor Microenvironment
    International Journal of Molecular Sciences Review Hold on or Cut? Integrin- and MMP-Mediated Cell–Matrix Interactions in the Tumor Microenvironment Stephan Niland and Johannes A. Eble * Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, 48149 Münster, Germany; [email protected] * Correspondence: [email protected] Abstract: The tumor microenvironment (TME) has become the focus of interest in cancer research and treatment. It includes the extracellular matrix (ECM) and ECM-modifying enzymes that are secreted by cancer and neighboring cells. The ECM serves both to anchor the tumor cells embedded in it and as a means of communication between the various cellular and non-cellular components of the TME. The cells of the TME modify their surrounding cancer-characteristic ECM. This in turn provides feedback to them via cellular receptors, thereby regulating, together with cytokines and exosomes, differentiation processes as well as tumor progression and spread. Matrix remodeling is accomplished by altering the repertoire of ECM components and by biophysical changes in stiffness and tension caused by ECM-crosslinking and ECM-degrading enzymes, in particular matrix metalloproteinases (MMPs). These can degrade ECM barriers or, by partial proteolysis, release soluble ECM fragments called matrikines, which influence cells inside and outside the TME. This review examines the changes in the ECM of the TME and the interaction between cells and the ECM, with a particular focus on MMPs. Keywords: tumor microenvironment; extracellular matrix; integrins; matrix metalloproteinases; matrikines Citation: Niland, S.; Eble, J.A. Hold on or Cut? Integrin- and MMP-Mediated Cell–Matrix 1. Introduction Interactions in the Tumor Microenvironment.
    [Show full text]
  • Human ADAM12 Quantikine ELISA
    Quantikine® ELISA Human ADAM12 Immunoassay Catalog Number DAD120 For the quantitative determination of A Disintegrin And Metalloproteinase domain- containing protein 12 (ADAM12) concentrations in cell culture supernates, serum, plasma, and urine. This package insert must be read in its entirety before using this product. For research use only. Not for use in diagnostic procedures. TABLE OF CONTENTS SECTION PAGE INTRODUCTION .....................................................................................................................................................................1 PRINCIPLE OF THE ASSAY ...................................................................................................................................................2 LIMITATIONS OF THE PROCEDURE .................................................................................................................................2 TECHNICAL HINTS .................................................................................................................................................................2 MATERIALS PROVIDED & STORAGE CONDITIONS ...................................................................................................3 OTHER SUPPLIES REQUIRED .............................................................................................................................................3 PRECAUTIONS .........................................................................................................................................................................4
    [Show full text]
  • Association of ADAM12 Gene Polymorphisms with Knee Osteoarthritis Susceptibility
    www.impactjournals.com/oncotarget/ Oncotarget, Supplementary Materials 2017 Association of ADAM12 gene polymorphisms with knee osteoarthritis susceptibility SUPPLEMENTARY MATERIALS REFERENCES candidate genes for the prevalence and progression of knee osteoarthritis. Arthritis Rheum. 2004;50:2497-2507. 1. Poonpet T, Tammachote R, Tammachote N, Kanitnate S, 11. Kerna I, Kisand K, Laitinen P, Tamm A, Tamm A. Honsawek S. Association between ADAM12 polymorphism Association of metallopeptidase domain 12 (ADAM12) and knee osteoarthritis in Thai population. Knee. gene polymorphisms and ADAM12 protein with the 2016;23:357-361. development of knee osteoarthritis. Osteoarthritis Cartilage. 2. Wang L, Guo L, Tian F, Hao R, Yang T. Analysis of single 2010;18. nucleotide polymorphisms within ADAM12 and risk of 12. Stark K, Straub RH, Blažičková S, Hengstenberg C, knee osteoarthritis in a Chinese Han population. Biomed Rovenský J. Genetics in neuroendocrine immunology: Res Int. 2015;2015:518643. implications for rheumatoid arthritis and osteoarthritis. Ann 3. Lou S, Zhao Z, Qian J, Zhao K, Wang R. Association N Y Acad Sci. 2010;1193. of single nucleotide polymorphisms in ADAM12 gene 13. Limer KL, Tosh K, Bujac SR, McConnell R, Doherty S, with susceptibility to kneeosteoarthritis: a case-control Nyberg F, Zhang W, Doherty M, Muir KR, Maciewicz study in a Chinese Han population. Int J Clin Exp Pathol. RA. Attempt to replicate published genetic associations 2014;7:5154-5159. in a large, well-defined osteoarthritis case-control 4. Kerna I, Kisand K, Tamm AE, Kumm J, Tamm AO. population (the GOAL study). Osteoarthritis Cartilage. Two single-nucleotide polymorphisms in ADAM12 2009;17:782-789. gene are associated with early and late radiographic 14.
    [Show full text]
  • ADAMTS13 and 15 Are Not Regulated by the Full Length and N‑Terminal Domain Forms of TIMP‑1, ‑2, ‑3 and ‑4
    BIOMEDICAL REPORTS 4: 73-78, 2016 ADAMTS13 and 15 are not regulated by the full length and N‑terminal domain forms of TIMP‑1, ‑2, ‑3 and ‑4 CENQI GUO, ANASTASIA TSIGKOU and MENG HUEE LEE Department of Biological Sciences, Xian Jiaotong-Liverpool University, Suzhou, Jiangsu 215123, P.R. China Received June 29, 2015; Accepted July 15, 2015 DOI: 10.3892/br.2015.535 Abstract. A disintegrin and metalloproteinase with thom- proteolysis activities associated with arthritis, morphogenesis, bospondin motifs (ADAMTS) 13 and 15 are secreted zinc angiogenesis and even ovulation [as reviewed previously (1,2)]. proteinases involved in the turnover of von Willebrand factor Also known as the VWF-cleaving protease, ADAMTS13 and cancer suppression. In the present study, ADAMTS13 is noted for its ability in cleaving and reducing the size of the and 15 were subjected to inhibition studies with the full-length ultra-large (UL) form of the VWF. Reduction in ADAMTS13 and N-terminal domain forms of tissue inhibitor of metallo- activity from either hereditary or acquired deficiency causes proteinases (TIMPs)-1 to -4. TIMPs have no ability to inhibit accumulation of UL-VWF multimers, platelet aggregation and the ADAMTS proteinases in the full-length or N-terminal arterial thrombosis that leads to fatal thrombotic thrombocy- domain form. While ADAMTS13 is also not sensitive to the topenic purpura [as reviewed previously (1,3)]. By contrast, hydroxamate inhibitors, batimastat and ilomastat, ADAMTS15 ADAMTS15 is a potential tumor suppressor. Only a limited app can be effectively inhibited by batimastat (Ki 299 nM). In number of in-depth investigations have been carried out on the conclusion, the present results indicate that TIMPs are not the enzyme; however, expression and profiling studies have shown regulators of these two ADAMTS proteinases.
    [Show full text]
  • ADAMTS Proteases in Vascular Biology
    Review MATBIO-1141; No. of pages: 8; 4C: 3, 6 ADAMTS proteases in vascular biology Juan Carlos Rodríguez-Manzaneque 1, Rubén Fernández-Rodríguez 1, Francisco Javier Rodríguez-Baena 1 and M. Luisa Iruela-Arispe 2 1 - GENYO, Centre for Genomics and Oncological Research, Pfizer, Universidad de Granada, Junta de Andalucía, 18016 Granada, Spain 2 - Department of Molecular, Cell, and Developmental Biology, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA Correspondence to Juan Carlos Rodríguez-Manzaneque and M. Luisa Iruela-Arispe: J.C Rodríguez-Manzaneque is to be contacted at: GENYO, 15 PTS Granada - Avda. de la Ilustración 114, Granada 18016, Spain; M.L. Iruela-Arispe, Department of Molecular, Cell and Developmental Biology, UCLA, 615 Charles Young Drive East, Los Angeles, CA 90095, USA. [email protected]; [email protected] http://dx.doi.org/10.1016/j.matbio.2015.02.004 Edited by W.C. Parks and S. Apte Abstract ADAMTS (a disintegrin and metalloprotease with thrombospondin motifs) proteases comprise the most recently discovered branch of the extracellular metalloenzymes. Research during the last 15 years, uncovered their association with a variety of physiological and pathological processes including blood coagulation, tissue repair, fertility, arthritis and cancer. Importantly, a frequent feature of ADAMTS enzymes relates to their effects on vascular-related phenomena, including angiogenesis. Their specific roles in vascular biology have been clarified by information on their expression profiles and substrate specificity. Through their catalytic activity, ADAMTS proteases modify rather than degrade extracellular proteins. They predominantly target proteoglycans and glycoproteins abundant in the basement membrane, therefore their broad contributions to the vasculature should not come as a surprise.
    [Show full text]
  • ADAMTS5 Assay, Human
    K-ASSAY KAMIKAMIYAYA BIOMEDICAL COMPANY KAMIYA BIOMEDICAL COMPANY ADAMTS5 Assay For the quantitative determination of human ADAMTS5 mRNA in whole blood, plasma, urine and transplantation tissue Cat. No. KT-697 For research use only, not for use in diagnostic procedures. 1 Revised 9815444 K-ASSAY KAMIKAMIYAYA BIOMEDICAL COMPANY PRODUCT INFORMATION ADAMTS5 Assay Cat. No. KT-697 PRODUCT The K-ASSAY ADAMTS5 Assay is a real time PCR assay for the quantitative determination of human ADAMTS5 (a disintegrin and metalloproteinase with thrombospondin motifs 5) mRNA in whole blood, plasma, urine and transplantation tissue. For research use only. Not for use in diagnostic procedures. INTRODUCTION Aggrecan is the major proteoglycan in cartilage, and is degraded by ADAMTS5 in arthritic cartilage. Studies in models of cultured bovine and porcine chondrocytes and cartilage explants have reported that ADAMTS5 is not induced by stimulation with IL-1 and TNF α. It has also been shown that ADAMTS5 expression in human synoviocytes is not inhibited by the anti-TNF biologics. PRINCIPLE ADAMTS5 TEST Kit contains specific primers, probes and calibrator DNA for the detection and quantification of human ADAMTS5 mRNA in samples. The test is based on real-time PCR that, in addition to specific forward and reverse oligonucleotide primers, utilizes MGB (minor groove binder) probe to generate a fluorescent signal when specific cDNA is present in samples. Samples, such as whole blood, plasma, urine, and transplantation tissue can be used. COMPONENTS Master Mix: 1 vial, 900 µL ADAMTS5 MGB Probe: 1 vial, 45 µL β-actin MGB Probe: 1 vial, 45 µL ADAMTS5 calibrator DNA: 1 vial, 50 µL β-actin calibrator DNA: 1 vial, 50 µL Each kit contains enough reagents to perform 21 tests.
    [Show full text]
  • Supplementary Table 1: Adhesion Genes Data Set
    Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like,
    [Show full text]
  • Serine Proteases with Altered Sensitivity to Activity-Modulating
    (19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants.
    [Show full text]
  • R&D Assay for Alzheimer's Disease
    R&DR&D assayassay forfor Alzheimer’sAlzheimer’s diseasedisease Target screening⳼ Ⲽ㬔 antibody array, ᢜ⭉㬔 ⸽ἐⴐ Amyloid β-peptide Alzheimer’s disease⯸ ኸᷠ᧔ ᆹ⸽ inhibitor, antibody, ELISA kit Surwhrph#Surilohu#Dqwlerg|#Duud| 6OUSFBUFE 1."5SFBUFE )41 $3&# &3, &3, )41 $3&# &3, &3, 壤伡庰䋸TBNQMF ɅH 侴䋸嵄䍴䋸BOBMZUFT䋸䬱娴哜塵 1$ 1$ 1$ 1$ 5IFNPTUSFGFSFODFEBSSBZT 1$ 1$ QQ α 34, .4, 503 Q α 34, .4, 503 %SVHTDSFFOJOH0òUBSHFUFòFDUT0ATHWAY涭廐 6OUSFBUFE 堄币䋸4BNQMF侴䋸8FTUFSOPS&-*4"䍘䧽 1."5SFBUFE P 8FTUFSOCMPU廽喜儤应侴䋸0, Z 4VCTUSBUF -JHIU )31DPOKVHBUFE1BO "OUJQIPTQIPUZSPTJOF .FBO1JYFM%FOTJUZ Y $BQUVSF"OUJCPEZ 5BSHFU"OBMZUF "SSBZ.FNCSBOF $3&# &3, &3, )41 .4, Q α 34, 503 Human XL Cytokine Array kit (ARY022, 102 analytes) Adiponectin,Aggrecan,Angiogenin,Angiopoietin-1,Angiopoietin-2,BAFF,BDNF,Complement,Component C5/C5a,CD14,CD30,CD40L, Chitinase 3-like 1,Complement Factor D,C-Reactive Protein,Cripto-1,Cystatin C,Dkk-1,DPPIV,EGF,EMMPRIN,ENA-78,Endoglin, Fas L,FGF basic,FGF- 7,FGF-19,Flt-3 L,G-CSF,GDF-15,GM-CSF,GRO-α,Grow th Hormone,HGF,ICAM-1,IFN-γ,IGFBP-2,IGFBP-3, IL-1α,IL-1β, IL-1ra,IL-2,IL-3,IL-4,IL- 5,IL-6,IL-8, IL-10,IL-11,IL-12, IL-13,IL-15,IL-16,IL-17A,IL-18 BPa,IL-19,IL-22, IL-23,IL-24,IL-27, IL-31,IL-32α/β/γ,IL-33,IL-34,IP-10,I-TAC,Kallikrein 3,Leptin,LIF,Lipocalin-2,MCP-1,MCP-3,M-CSF,MIF,MIG,MIP-1α/MIP-1β,MIP-3α,MIP-3β,MMP-9, Myeloperoxidase,Osteopontin, p70, PDGF-AA, PDGF-AB/BB,Pentraxin-3, PF4, RAGE, RANTES,RBP4,Relaxin-2, Resistin,SDF-1α,Serpin E1, SHBG, ST2, TARC,TFF3,TfR,TGF- ,Thrombospondin-1,TNF-α, uPAR, VEGF, Vitamin D BP Human Protease (34 analytes) /
    [Show full text]
  • Gene Symbol Category ACAN ECM ADAM10 ECM Remodeling-Related ADAM11 ECM Remodeling-Related ADAM12 ECM Remodeling-Related ADAM15 E
    Supplementary Material (ESI) for Integrative Biology This journal is (c) The Royal Society of Chemistry 2010 Gene symbol Category ACAN ECM ADAM10 ECM remodeling-related ADAM11 ECM remodeling-related ADAM12 ECM remodeling-related ADAM15 ECM remodeling-related ADAM17 ECM remodeling-related ADAM18 ECM remodeling-related ADAM19 ECM remodeling-related ADAM2 ECM remodeling-related ADAM20 ECM remodeling-related ADAM21 ECM remodeling-related ADAM22 ECM remodeling-related ADAM23 ECM remodeling-related ADAM28 ECM remodeling-related ADAM29 ECM remodeling-related ADAM3 ECM remodeling-related ADAM30 ECM remodeling-related ADAM5 ECM remodeling-related ADAM7 ECM remodeling-related ADAM8 ECM remodeling-related ADAM9 ECM remodeling-related ADAMTS1 ECM remodeling-related ADAMTS10 ECM remodeling-related ADAMTS12 ECM remodeling-related ADAMTS13 ECM remodeling-related ADAMTS14 ECM remodeling-related ADAMTS15 ECM remodeling-related ADAMTS16 ECM remodeling-related ADAMTS17 ECM remodeling-related ADAMTS18 ECM remodeling-related ADAMTS19 ECM remodeling-related ADAMTS2 ECM remodeling-related ADAMTS20 ECM remodeling-related ADAMTS3 ECM remodeling-related ADAMTS4 ECM remodeling-related ADAMTS5 ECM remodeling-related ADAMTS6 ECM remodeling-related ADAMTS7 ECM remodeling-related ADAMTS8 ECM remodeling-related ADAMTS9 ECM remodeling-related ADAMTSL1 ECM remodeling-related ADAMTSL2 ECM remodeling-related ADAMTSL3 ECM remodeling-related ADAMTSL4 ECM remodeling-related ADAMTSL5 ECM remodeling-related AGRIN ECM ALCAM Cell-cell adhesion ANGPT1 Soluble factors and receptors
    [Show full text]
  • Pharmnotes February 2019
    PharmNOTES Summary about new FDA products, generic medication, medical products, and WHAT IS IN THE PIPELINE. From: FEBRUARY 2019 Date: 3/7/2019 ©2019 PharmPiX. All rights reserved Table of Contents Page News 3 New FDA Approved Products 4-12 Jeuveau™ (prabotulinumtoxinA-xvfs) 4-5 Cablivi™ (caplacizumab-yhdp) 6-8 Egaten™ (triclabendazole) 9-10 Esperoct™ (turoctocog alfa pegol) 11-12 New FDA Approved Indications 13-14 New FDA Approved Dosage Forms, Formulations, Combinations, and Other Differences 15 New First-Time Generic Drug Approval 16 Pipeline 17-18 References 19 2 NEWS………………………… Drug Issue Date News/Event Increased risk of 02/21/2019 The FDA has concluded that there is an increased risk of death with Uloric (febuxostat) compared to another gout medicine, death with Uloric™ allopurinol. As a result, the Uloric™ prescribing information will include a Boxed Warning. The FDA is also limiting the (febuxostat) approved use of Uloric™ to certain patients who are not treated effectively or experience severe side effects with allopurinol. Recommendations for healthcare professionals: • Reserve Uloric™ for use only in patients who have failed or do not tolerate allopurinol. • Counsel patients about the cardiovascular risk with Uloric™ and advise them to seek medical attention immediately if they experience the following symptoms: chest pain, shortness of breath, rapid or irregular heartbeat, numbness or weakness on one side of the body, dizziness, trouble talking, sudden severe headache. For more details regarding this safety issue, please visit: https://www.fda.gov/Drugs/DrugSafety/ucm631182.htm Risk of blood clots in 02/25/2019 The FDA is alerting the public that a safety clinical trial found an increased risk of blood clots in the lungs and death when a 10 the lungs and death mg twice daily dose of tofacitinib (Xeljanz™, Xeljanz XR™) was used in patients with rheumatoid arthritis (RA).
    [Show full text]