Human PPIL1 Protein (His Tag)

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Human PPIL1 Protein (His Tag) Catalog Number: 14163-H08E General Information SDS-PAGE: Gene Name Synonym: CGI-124; CYPL1; hCyPX; PPIase Protein Construction: A DNA sequence encoding the human PPIL1 (Q9Y3C6) (Met1-Gly166) was expressed with a polyhistidine tag at the C-terminus. Source: Human Expression Host: E. coli QC Testing Purity: > 90 % as determined by SDS-PAGE Endotoxin: Protein Description Please contact us for more information. PPIL1 is a member of the cyclophilin family. Cyclophilins are well Stability: conserved and ubiquitous. Members of cyclophilin family take an significant part in protein folding, immunosuppression by cyclosporin A, and infection Samples are stable for up to twelve months from date of receipt at -70 ℃ of HIV-1 virions. PPIL1 is a peptidylprolyl isomerase(PPIase). It increases the folding of proteins and catalyze the cis-trans isomerization of proline Predicted N terminal: Met imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of Molecular Mass: cancer cells through modulation of phosphorylation of stathmin. It is a novel molecular target for colon-cancer therapy. The recombinant human PPIL1 consists of 172 amino acids and predicts a molecular mass of 19.1 KDa. It migrates as an approximately 17 - 20 KDa References band in SDS-PAGE under reducing conditions. 1.Xu C. et al., 2005, J Biomol NMR. 31 (2): 179-80. 2.Ozaki K. et al., 1997, Formulation: Cytogenet Cell Genet. 72 (2-3): 242-5. 3.Mann SS. et al., 1999, Cytogenet Cell Genet. 83 (3-4): 228-9. Lyophilized from sterile 50mM Tris, 10% glycerol, pH 8.0 Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. Please contact us for any concerns or special requirements. Usage Guide Storage: Store it under sterile conditions at -20℃ to -80℃ upon receiving. Recommend to aliquot the protein into smaller quantities for optimal storage. Avoid repeated freeze-thaw cycles. Reconstitution: Detailed reconstitution instructions are sent along with the products. Manufactured By Sino Biological Inc., FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS. For US Customer： Fax: 267-657-0217 Tel：215-583-7898 Global Customer： Fax :+86-10-5862-8288 Tel:+86-400-890-9989 http://www.sinobiological.com.

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32-2709: PPIL1 Recombinant Protein Description Product Info Application
9853 Pacific Heights Blvd. Suite D. San Diego, CA 92121, USA Tel: 858-263-4982 Email: [email protected] 32-2709: PPIL1 Recombinant Protein Alternative Name : Peptidyl-Prolyl Cis-Trans Isomerase-Like 1,PPIL-1,CYPL1,hCyPX,MGC678,PPIase,CGI-124,PPIL1. Description Source : Escherichia Coli. PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques. PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon- cancer therapy. Product Info Amount : 50 µg Purification : Greater than 95.0% as determined by SDS-PAGE. Content : PPIL1 solution containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol PPIL1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below Storage condition : -18°C. Please prevent freeze thaw cycles. Amino Acid : MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH. Application Note Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.
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In This Table Protein Name, Uniprot Code, Gene Name P-Value
Supplementary Table S1: In this table protein name, uniprot code, gene name p-value and Fold change (FC) for each comparison are shown, for 299 of the 301 significantly regulated proteins found in both comparisons (p-value<0.01, fold change (FC) >+/-0.37) ALS versus control and FTLD-U versus control. Two uncharacterized proteins have been excluded from this list Protein name Uniprot Gene name p value FC FTLD-U p value FC ALS FTLD-U ALS Cytochrome b-c1 complex P14927 UQCRB 1.534E-03 -1.591E+00 6.005E-04 -1.639E+00 subunit 7 NADH dehydrogenase O95182 NDUFA7 4.127E-04 -9.471E-01 3.467E-05 -1.643E+00 [ubiquinone] 1 alpha subcomplex subunit 7 NADH dehydrogenase O43678 NDUFA2 3.230E-04 -9.145E-01 2.113E-04 -1.450E+00 [ubiquinone] 1 alpha subcomplex subunit 2 NADH dehydrogenase O43920 NDUFS5 1.769E-04 -8.829E-01 3.235E-05 -1.007E+00 [ubiquinone] iron-sulfur protein 5 ARF GTPase-activating A0A0C4DGN6 GIT1 1.306E-03 -8.810E-01 1.115E-03 -7.228E-01 protein GIT1 Methylglutaconyl-CoA Q13825 AUH 6.097E-04 -7.666E-01 5.619E-06 -1.178E+00 hydratase, mitochondrial ADP/ATP translocase 1 P12235 SLC25A4 6.068E-03 -6.095E-01 3.595E-04 -1.011E+00 MIC J3QTA6 CHCHD6 1.090E-04 -5.913E-01 2.124E-03 -5.948E-01 MIC J3QTA6 CHCHD6 1.090E-04 -5.913E-01 2.124E-03 -5.948E-01 Protein kinase C and casein Q9BY11 PACSIN1 3.837E-03 -5.863E-01 3.680E-06 -1.824E+00 kinase substrate in neurons protein 1 Tubulin polymerization- O94811 TPPP 6.466E-03 -5.755E-01 6.943E-06 -1.169E+00 promoting protein MIC C9JRZ6 CHCHD3 2.912E-02 -6.187E-01 2.195E-03 -9.781E-01 Mitochondrial 2-
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Frontiers Medicine Csa 2021
1 Frontiers Medicine 2 February 3, 2021 3 Title: Cyclosporin A: a repurposable drug in the treatment of COVID-19 ? 4 5 Running title: Cyclosporin A and COVID-19 6 7 Christian A. DEVAUX,1,2*, Cléa MELENOTTE1, Marie-Dominique 8 PIERCECCHI-MARTI3,4, Clémence DELTEIL3,4, and Didier RAOULT1 9 10 1Aix-Marseille Univ, IRD, APHM, MEPHI, IHU-Méditerranée Infection, Marseille, 11 France 12 2 CNRS, Marseille, France 13 3 Department of Legal Medicine, Hôpital de la Timone, Marseille University Hospital 14 Center, Marseille, France 15 4 Aix Marseille Univ, CNRS, EFS, ADES, Marseille, France 16 17 *Corresponding author : 18 Christian Devaux, PhD 19 IHU Méditerranée Infection, 19-21 Boulevard Jean Moulin, 13385 Marseille, France 20 Phone: (+33) 4 13 73 20 51 21 Fax : (+33) 4 13 73 20 52 22 E-mail: [email protected] 23 24 Abstract length: 190 words; Manuscript length:,7817 words 25 Figures: 7 26 Table 4 27 Keywords: SARS-CoV-2; COVID-19; Cyclosporin A; Cyclophilin; ACE2 28 Summary: 29 COVID-19 is now at the forefront of major health challenge faced globally, creating an urgent 30 need for safe and efficient therapeutic strategies. Given the high attrition rates, high costs and 31 quite slow development of drug discovery, repurposing of known FDA-approved molecules is 32 increasingly becoming an attractive issue in order to quickly find molecules capable of 33 preventing and/or curing COVID-19 patients. Cyclosporin A (CsA), a common anti-rejection 34 drug widely used in transplantation, has recently been shown to exhibit substantial anti- 35 SARS-CoV-2 antiviral activity and anti-COVID-19 effect.
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Transcriptome Analysis of Paralichthys Olivaceus Erythrocytes Reveals Profound Immune Responses Induced by Edwardsiella Tarda Infection
International Journal of Molecular Sciences Article Transcriptome Analysis of Paralichthys olivaceus Erythrocytes Reveals Profound Immune Responses Induced by Edwardsiella tarda Infection Bin Sun 1,2,3 , Xuepeng Li 1, Xianhui Ning 1 and Li Sun 1,2,* 1 CAS Key Laboratory of Experimental Marine Biology, CAS Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, Qingdao 266071, China; [email protected] (B.S.); [email protected] (X.L.); [email protected] (X.N.) 2 Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, 1 Wenhai Road, Qingdao 266237, China 3 University of Chinese Academy of Sciences, 19 Yuquan Road, Beijing 100049, China * Correspondence: [email protected]; Tel.: +86-532-82898829 Received: 13 March 2020; Accepted: 3 April 2020; Published: 28 April 2020 Abstract: Unlike mammalian red blood cells (RBCs), fish RBCs are nucleated and thus capable of gene expression. Japanese flounder (Paralichthys olivaceus) is a species of marine fish with important economic values. Flounder are susceptible to Edwardsiella tarda, a severe bacterial pathogen that is able to infect and survive in flounder phagocytes. However, the infectivity of and the immune response induced by E. tarda in flounder RBCs are unclear. In the present research, we found that E. tarda was able to invade and replicate inside flounder RBCs in both in vitro and in vivo infections. To investigate the immune response induced by E. tarda in RBCs, transcriptome analysis of the spleen RBCs of flounder challenged with E. tarda was performed. Six sequencing libraries were constructed, and an average of 43 million clean reads per library were obtained, with 85% of the reads being successfully mapped to the genome of flounder.
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Immunosuppression by Cyclosporine Cyclophilin A-Deficient Mice Are
Cyclophilin A-Deficient Mice Are Resistant to Immunosuppression by Cyclosporine John Colgan, Mohammed Asmal, Bin Yu and Jeremy Luban This information is current as J Immunol 2005; 174:6030-6038; ; of October 2, 2021. doi: 10.4049/jimmunol.174.10.6030 http://www.jimmunol.org/content/174/10/6030 References This article cites 53 articles, 28 of which you can access for free at: Downloaded from http://www.jimmunol.org/content/174/10/6030.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision http://www.jimmunol.org/ • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: by guest on October 2, 2021 http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2005 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Cyclophilin A-Deﬁcient Mice Are Resistant to Immunosuppression by Cyclosporine1 John Colgan,2* Mohammed Asmal,* Bin Yu,* and Jeremy Luban3*† Cyclosporine is an immunosuppressive drug that is widely used to prevent organ transplant rejection. Known intracellular ligands for cyclosporine include the cyclophilins, a large family of phylogenetically conserved proteins that potentially regulate protein folding in cells.
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Structural and Functional Insights Into Human Nuclear Cyclophilins
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 2 November 2018 doi:10.20944/preprints201811.0037.v1 Peer-reviewed version available at Biomolecules 2018, 8, 161; doi:10.3390/biom8040161 1 Review 2 Structural and Functional Insights into Human 3 Nuclear Cyclophilins 4 Caroline Rajiv12 and Tara L. Davis13,* 5 1 Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, 6 Philadelphia PA USA 19102. 7 2 Janssen Pharmaceuticals, Inc., 22-21062, 1400 McKean Rd, Spring House, PA 19477; 8 [email protected] 9 3 FORMA Therapeutics, 550 Arsenal St. Ste. 100, Boston, MA 02472; [email protected] 10 11 * Correspondence: [email protected]; Tel.: +01-857-209-2342 12 13 Abstract: The peptidyl-prolyl isomerases of the cyclophilin type are distributed throughout human 14 cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes 15 that regulate chromatin modification, transcription, and pre-mRNA splicing. This review collects 16 what is known about the eight human nuclear cyclophilins: PPIH, PPIE, PPIL1, PPIL2, PPIL3, PPIG, 17 CWC27, and PPWD1. Each “spliceophilin” is evaluated in relation to the spliceosomal complex in 18 which it has been studied, and current work studying the biological roles of these cyclophilins in 19 the nucleus are discussed. The eight human splicing complexes available in the RCSB are analyzed 20 from the viewpoint of the human spliceophilins. Future directions in structural and cellular biology, 21 and the importance of developing spliceophilin-specific inhibitors, are considered. 22 23 Keywords: Peptidyl-prolyl isomerases; nuclear cyclophilins; spliceophilins; alternative splicing; 24 spliceosomes; NMR; x-ray crystallography 25 26 27 1.
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Cyclophilins As Modulators of Viral Replication
Viruses 2013, 5, 1684-1701; doi:10.3390/v5071684 OPEN ACCESS viruses ISSN 1999-4915 www.mdpi.com/journal/viruses Review Cyclophilins as Modulators of Viral Replication Stephen D. Frausto, Emily Lee and Hengli Tang * Department of Biological Science, The Florida State University, Tallahassee, FL 32306, USA; E-Mails: [email protected] (S.D.F); [email protected] (E.L.) * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +1-850-645-2402; Fax: +1-850-645-8447. Received: 22 May 2013; in revised form: 26 June 2013 / Accepted: 3 July 2013 / Published: 11 July 2013 Abstract: Cyclophilins are peptidyl‐prolyl cis/trans isomerases important in the proper folding of certain proteins. Mounting evidence supports varied roles of cyclophilins, either positive or negative, in the life cycles of diverse viruses, but the nature and mechanisms of these roles are yet to be defined. The potential for cyclophilins to serve as a drug target for antiviral therapy is evidenced by the success of non-immunosuppressive cyclophilin inhibitors (CPIs), including Alisporivir, in clinical trials targeting hepatitis C virus infection. In addition, as cyclophilins are implicated in the predisposition to, or severity of, various diseases, the ability to specifically and effectively modulate their function will prove increasingly useful for disease intervention. In this review, we will summarize the evidence of cyclophilins as key mediators of viral infection and prospective drug targets. Keywords: cyclosporin; HIV; HCV; cyclophilin 1. Introduction Unlike other infective agents, viruses do not encode a full complement of proteins that allow them to proliferate independent of the host.
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UC San Diego Electronic Theses and Dissertations
UC San Diego UC San Diego Electronic Theses and Dissertations Title Cardiac Stretch-Induced Transcriptomic Changes are Axis-Dependent Permalink https://escholarship.org/uc/item/7m04f0b0 Author Buchholz, Kyle Stephen Publication Date 2016 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California UNIVERSITY OF CALIFORNIA, SAN DIEGO Cardiac Stretch-Induced Transcriptomic Changes are Axis-Dependent A dissertation submitted in partial satisfaction of the requirements for the degree Doctor of Philosophy in Bioengineering by Kyle Stephen Buchholz Committee in Charge: Professor Jeffrey Omens, Chair Professor Andrew McCulloch, Co-Chair Professor Ju Chen Professor Karen Christman Professor Robert Ross Professor Alexander Zambon 2016 Copyright Kyle Stephen Buchholz, 2016 All rights reserved Signature Page The Dissertation of Kyle Stephen Buchholz is approved and it is acceptable in quality and form for publication on microfilm and electronically: Co-Chair Chair University of California, San Diego 2016 iii Dedication To my beautiful wife, Rhia. iv Table of Contents Signature Page ................................................................................................................... iii Dedication .......................................................................................................................... iv Table of Contents ................................................................................................................ v List of Figures ...................................................................................................................
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ZBTB33 Is Mutated in Clonal Hematopoiesis and Myelodysplastic Syndromes and Impacts RNA Splicing
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Structural and Functional Insights Into Human Nuclear Cyclophilins
biomolecules Review Structural and Functional Insights into Human Nuclear Cyclophilins Caroline Rajiv 1,2 and Tara L. Davis 1,3,* 1 Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USA; [email protected] 2 Janssen Pharmaceuticals Inc., 22-21062, 1400 McKean Rd, Spring House, PA 19477, USA 3 FORMA Therapeutics, 550 Arsenal St. Ste. 100, Boston, MA 02472, USA * Correspondence: [email protected]; Tel.: +1-857-209-2342 Received: 31 October 2018; Accepted: 22 November 2018; Published: 4 December 2018 Abstract: The peptidyl prolyl isomerases (PPI) of the cyclophilin type are distributed throughout human cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes that regulate chromatin modiﬁcation, transcription, and pre-mRNA splicing. This review collects what is known about the eight human nuclear cyclophilins: peptidyl prolyl isomerase H (PPIH), peptidyl prolyl isomerase E (PPIE), peptidyl prolyl isomerase-like 1 (PPIL1), peptidyl prolyl isomerase-like 2 (PPIL2), peptidyl prolyl isomerase-like 3 (PPIL3), peptidyl prolyl isomerase G (PPIG), spliceosome-associated protein CWC27 homolog (CWC27), and peptidyl prolyl isomerase domain and WD repeat-containing protein 1 (PPWD1). Each “spliceophilin” is evaluated in relation to the spliceosomal complex in which it has been studied, and current work studying the biological roles of these cyclophilins in the nucleus are discussed. The eight human splicing complexes available in the Protein Data Bank (PDB) are analyzed from the viewpoint of the human spliceophilins. Future directions in structural and cellular biology, and the importance of developing spliceophilin-speciﬁc inhibitors, are considered. Keywords: peptidyl prolyl isomerases; nuclear cyclophilins; spliceophilins; alternative splicing; spliceosomes; NMR; X-ray crystallography 1.
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Peripheral Nerve Single-Cell Analysis Identifies Mesenchymal Ligands That Promote Axonal Growth
Research Article: New Research Development Peripheral Nerve Single-Cell Analysis Identifies Mesenchymal Ligands that Promote Axonal Growth Jeremy S. Toma,1 Konstantina Karamboulas,1,ª Matthew J. Carr,1,2,ª Adelaida Kolaj,1,3 Scott A. Yuzwa,1 Neemat Mahmud,1,3 Mekayla A. Storer,1 David R. Kaplan,1,2,4 and Freda D. Miller1,2,3,4 https://doi.org/10.1523/ENEURO.0066-20.2020 1Program in Neurosciences and Mental Health, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada, 2Institute of Medical Sciences University of Toronto, Toronto, Ontario M5G 1A8, Canada, 3Department of Physiology, University of Toronto, Toronto, Ontario M5G 1A8, Canada, and 4Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5G 1A8, Canada Abstract Peripheral nerves provide a supportive growth environment for developing and regenerating axons and are es- sential for maintenance and repair of many non-neural tissues. This capacity has largely been ascribed to paracrine factors secreted by nerve-resident Schwann cells. Here, we used single-cell transcriptional profiling to identify ligands made by different injured rodent nerve cell types and have combined this with cell-surface mass spectrometry to computationally model potential paracrine interactions with peripheral neurons. These analyses show that peripheral nerves make many ligands predicted to act on peripheral and CNS neurons, in- cluding known and previously uncharacterized ligands. While Schwann cells are an important ligand source within injured nerves, more than half of the predicted ligands are made by nerve-resident mesenchymal cells, including the endoneurial cells most closely associated with peripheral axons. At least three of these mesen- chymal ligands, ANGPT1, CCL11, and VEGFC, promote growth when locally applied on sympathetic axons.
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Primepcr™Assay Validation Report
PrimePCR™Assay Validation Report Gene Information Gene Name peptidylprolyl isomerase (cyclophilin)-like 1 Gene Symbol PPIL1 Organism Human Gene Summary This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved ubiquitous family members of which play an important role in protein folding immunosuppression by cyclosporin A and infection of HIV-1 virions. Based on similarity to other PPIases this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Gene Aliases CYPL1, MGC678, PPIase, hCyPX RefSeq Accession No. NC_000006.11, NT_007592.15 UniGene ID Hs.27693 Ensembl Gene ID ENSG00000137168 Entrez Gene ID 51645 Assay Information Unique Assay ID qHsaCEP0052014 Assay Type Probe - Validation information is for the primer pair using SYBR® Green detection Detected Coding Transcript(s) ENST00000373699 Amplicon Context Sequence ATGCCAGGCCTCCTAAGCTTCATGACTTGCAAAGCCAAAATGAATTTAGCATTAC ATGTCATTCTATGTCATCTAGAAGCTGGTTCACTGGGGCCATCTCAGAAGAGCTG CTCAAGAGGGTAGCAAGTCTACCCAGA Amplicon Length (bp) 107 Chromosome Location 6:36823461-36823597 Assay Design Exonic Purification Desalted Validation Results Efficiency (%) 100 R2 1 cDNA Cq 20.01 cDNA Tm (Celsius) 80.5 Page 1/5 PrimePCR™Assay Validation Report gDNA Cq 24.14 Specificity (%) 100 Information to assist with data interpretation is provided at the end of this report. Page 2/5 PrimePCR™Assay Validation Report PPIL1, Human Amplification Plot Amplification
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