PPIE Antibody Cat

Total Page：16

File Type：pdf, Size：1020Kb

PPIE Antibody Cat. No.: 29-363 PPIE Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Dog, Drosophila, Human, Mouse, Rat, Zebrafish Antibody produced in rabbits immunized with a synthetic peptide corresponding a region IMMUNOGEN: of human PPIE. TESTED APPLICATIONS: ELISA, WB PPIE antibody can be used for detection of PPIE by ELISA at 1:312500. PPIE antibody can APPLICATIONS: be used for detection of PPIE by western blot at 2.5 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000. POSITIVE CONTROL: 1) Cat. No. 1205 - Jurkat Cell Lysate PREDICTED MOLECULAR 26 kDa, 33 kDa, 33 kDa WEIGHT: Properties PURIFICATION: Antibody is purified by protein A chromatography method. CLONALITY: Polyclonal CONJUGATE: Unconjugated PHYSICAL STATE: Liquid September 29, 2021 1 https://www.prosci-inc.com/ppie-antibody-29-363.html Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% BUFFER: sucrose. CONCENTRATION: batch dependent For short periods of storage (days) store at 4˚C. For longer periods of storage, store PPIE STORAGE CONDITIONS: antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: PPIE ALTERNATE NAMES: PPIE, CYP33, CYP-33 ACCESSION NO.: NP_982282 PROTEIN GI NO.: 45439318 GENE ID: 10450 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activityThe protein encoded by this BACKGROUND: gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed. REFERENCES: 1) Fair, K., (2001) Mol. Cell. Biol. 21 (10), 3589-3597. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 29, 2021 2 https://www.prosci-inc.com/ppie-antibody-29-363.html.

Copy Link

Recommended publications

Identification of the Binding Partners for Hspb2 and Cryab Reveals
Brigham Young University BYU ScholarsArchive Theses and Dissertations 2013-12-12 Identification of the Binding arP tners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactions and Non- Redundant Roles for Small Heat Shock Proteins Kelsey Murphey Langston Brigham Young University - Provo Follow this and additional works at: https://scholarsarchive.byu.edu/etd Part of the Microbiology Commons BYU ScholarsArchive Citation Langston, Kelsey Murphey, "Identification of the Binding Partners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactions and Non-Redundant Roles for Small Heat Shock Proteins" (2013). Theses and Dissertations. 3822. https://scholarsarchive.byu.edu/etd/3822 This Thesis is brought to you for free and open access by BYU ScholarsArchive. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of BYU ScholarsArchive. For more information, please contact [email protected], [email protected]. Identification of the Binding Partners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactions and Non-Redundant Roles for Small Heat Shock Proteins Kelsey Langston A thesis submitted to the faculty of Brigham Young University in partial fulfillment of the requirements for the degree of Master of Science Julianne H. Grose, Chair William R. McCleary Brian Poole Department of Microbiology and Molecular Biology Brigham Young University December 2013 Copyright © 2013 Kelsey Langston All Rights Reserved ABSTRACT Identification of the Binding Partners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactors and Non-Redundant Roles for Small Heat Shock Proteins Kelsey Langston Department of Microbiology and Molecular Biology, BYU Master of Science Small Heat Shock Proteins (sHSP) are molecular chaperones that play protective roles in cell survival and have been shown to possess chaperone activity.
[Show full text]
Alternative Cleavage and Polyadenylation During Colorectal Cancer Development
Author Manuscript Published OnlineFirst on August 8, 2012; DOI: 10.1158/1078-0432.CCR-12-0543 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Alternative cleavage and polyadenylation during colorectal cancer development Adam R. Morris1#, Arnold Bos1#, Begoña Diosdado2, Koos Rooijers1, Ran Elkon1, Anne S. Bolijn2, Beatriz Carvalho2, Gerrit A. Meijer2, and Reuven Agami1,3$ 1. Division of Gene Regulation, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, The Netherlands 2. Department of Pathology VU medical centre, De Boelelaan 1117, 1081HV Amsterdam, The Netherlands 3. The Centre for Biomedical Genetics, The Netherlands Running Title: Alternative polyadenylation in colorectal cancer Keywords: Alternative cleavage and polyadenylation, colorectal cancer, next generation sequencing, Adenoma, carcinoma Conflicts of interest: none Word count: 4055 Tables: 2; Figures: 3 # These authors contributed equally to this work $Email: [email protected] Tel. +31(0)20 512 2079 Fax. +31(0)20 512 1999 Downloaded from clincancerres.aacrjournals.org on September 28, 2021. © 2012 American Association for Cancer Research. Author Manuscript Published OnlineFirst on August 8, 2012; DOI: 10.1158/1078-0432.CCR-12-0543 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. ABSTRACT Purpose: Alternative cleavage and polyadenylation (APA) of mRNAs is a phenomenon that alters 3'-untranslated region length leading to altered posttranscriptional regulation of gene expression. Changing APA patterns have been shown to result in mis-regulation of genes involved in carcinogenesis, therefore we hypothesized that altered APA contributes to progression of colorectal cancer, and that measurement of APA may lead to discovery of novel biomarkers.
[Show full text]
Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins
Technical note Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl cis/trans Isomerases (PPIase) Andrzej Galat Retired from: Service d’Ingénierie Moléculaire des Protéines (SIMOPRO), CEA-Université Paris-Saclay, France; [email protected]; Tel.: +33-0164465072 Received: 21 December 2018; Accepted: 21 January 2019; Published: 11 February 2019 Abstract: In this technical note, we describe analyses of more than 15,000 sequences of FK506- binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl cis/trans isomerases (PPIases). We have developed a novel way of displaying relative changes of amino acid (AA)- residues at a given sequence position by using heat-maps. This type of representation allows simultaneous estimation of conservation level in a given sequence position in the entire group of functionally-related paralogues (multigene family of proteins). We have also proposed that at least two FKBPs, namely FKBP36, encoded by the Fkbp6 gene and FKBP51, encoded by the Fkbp5 gene, can form dimers bound via a disulfide bridge in the nucleus. This type of dimer may have some crucial function in the regulation of some nuclear complexes at different stages of the cell cycle. Keywords: FKBP; cyclophilin; PPIase; heat-map; immunophilin 1 Introduction About 30 years ago, an exciting adventure began in finding some correlations between pharmacological activities of macrocyclic hydrophobic drugs, namely the cyclic peptide cyclosporine A (CsA), and two macrolides, namely FK506 and rapamycin, which have profound and clinically useful immunosuppressive effects, especially in organ transplantations and in combating some immune disorders.
[Show full text]
Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
cells Review Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin Agnieszka Bochy ńska,Juliane Lüscher-Firzlaff and Bernhard Lüscher * ID Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Pauwelsstrasse 30, 52057 Aachen, Germany; [email protected] (A.B.); jluescher-fi[email protected] (J.L.-F.) * Correspondence: [email protected]; Tel.: +49-241-8088850; Fax: +49-241-8082427 Received: 18 January 2018; Accepted: 27 February 2018; Published: 2 March 2018 Abstract: Regulation of gene expression is achieved by sequence-specific transcriptional regulators, which convey the information that is contained in the sequence of DNA into RNA polymerase activity. This is achieved by the recruitment of transcriptional co-factors. One of the consequences of co-factor recruitment is the control of specific properties of nucleosomes, the basic units of chromatin, and their protein components, the core histones. The main principles are to regulate the position and the characteristics of nucleosomes. The latter includes modulating the composition of core histones and their variants that are integrated into nucleosomes, and the post-translational modification of these histones referred to as histone marks. One of these marks is the methylation of lysine 4 of the core histone H3 (H3K4). While mono-methylation of H3K4 (H3K4me1) is located preferentially at active enhancers, tri-methylation (H3K4me3) is a mark found at open and potentially active promoters. Thus, H3K4 methylation is typically associated with gene transcription. The class 2 lysine methyltransferases (KMTs) are the main enzymes that methylate H3K4. KMT2 enzymes function in complexes that contain a necessary core complex composed of WDR5, RBBP5, ASH2L, and DPY30, the so-called WRAD complex.
[Show full text]
Aberrant Activity of Histone–Lysine N-Methyltransferase 2 (KMT2) Complexes in Oncogenesis
International Journal of Molecular Sciences Review Aberrant Activity of Histone–Lysine N-Methyltransferase 2 (KMT2) Complexes in Oncogenesis Elzbieta Poreba 1,* , Krzysztof Lesniewicz 2 and Julia Durzynska 1,* 1 Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University, ul. Uniwersytetu Poznańskiego6, 61-614 Poznań,Poland 2 Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, ul. Uniwersytetu Poznańskiego6, 61-614 Poznań,Poland; [email protected] * Correspondence: [email protected] (E.P.); [email protected] (J.D.); Tel.: +48-61-829-5857 (E.P.) Received: 19 November 2020; Accepted: 6 December 2020; Published: 8 December 2020 Abstract: KMT2 (histone-lysine N-methyltransferase subclass 2) complexes methylate lysine 4 on the histone H3 tail at gene promoters and gene enhancers and, thus, control the process of gene transcription. These complexes not only play an essential role in normal development but have also been described as involved in the aberrant growth of tissues. KMT2 mutations resulting from the rearrangements of the KMT2A (MLL1) gene at 11q23 are associated with pediatric mixed-lineage leukemias, and recent studies demonstrate that KMT2 genes are frequently mutated in many types of human cancers. Moreover, other components of the KMT2 complexes have been reported to contribute to oncogenesis. This review summarizes the recent advances in our knowledge of the role of KMT2 complexes in cell transformation. In addition, it discusses the therapeutic targeting of different components of the KMT2 complexes. Keywords: histone–lysine N-methyltransferase 2; COMPASS; COMPASS-like; H3K4 methylation; oncogenesis; cancer; epigenetics; chromatin 1.
[Show full text]
Anti-PPIE Antibody [17E8] (ARG57492)
Product datasheet [email protected] ARG57492 Package: 50 μl anti-PPIE antibody [17E8] Store at: -20°C Summary Product Description Mouse Monoclonal antibody [17E8] recognizes PPIE Tested Reactivity Hu Tested Application WB Host Mouse Clonality Monoclonal Clone 17E8 Isotype IgG1, kappa Target Name PPIE Antigen Species Human Immunogen Recombinant Human PPIE (aa. 1-301aa) purified from E. coli. Conjugation Un-conjugated Alternate Names Cyclophilin-33; CYP-33; Cyclophilin E; PPIase E; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase E; CYP33; Rotamase E Application Instructions Application table Application Dilution WB 1:1000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 33 kDa Properties Form Liquid Purification Purification with Protein A. Buffer PBS (pH 7.4), 0.02% Sodium azide and 10% Glycerol. Preservative 0.02% Sodium azide Stabilizer 10% Glycerol Concentration 1 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol PPIE Gene Full Name peptidylprolyl isomerase E (cyclophilin E) Background The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins.
[Show full text]
Anti-PPIE (GW22196)
3050 Spruce Street, Saint Louis, MO 63103 USA Tel: (800) 521-8956 (314) 771-5765 Fax: (800) 325-5052 (314) 771-5757 email: [email protected] Product Information Anti-PPIE antibody produced in chicken, affinity isolated antibody Catalog Number GW22196 Formerly listed as GenWay Catalog Number 15-288-22196, Peptidyl-prolyl cis-trans isomerase Antibody. – Storage Temperature Store at 20 °C The product is a clear, colorless solution in phosphate buffered saline, pH 7.2, containing 0.02% sodium azide. Synonyms: Peptidylprolyl isomerase E isoform 1, EC 5.2.1.8 Species Reactivity: Human, mouse, rat Product Description PPIases accelerate the folding of proteins.The protein Tested Applications: WB encoded by this gene is a member of the peptidyl-prolyl Recommended Dilutions: Recommended starting dilution cis-trans isomerase (PPIase) family. PPIases catalyze the cis- for Western blot analysis is 1:500, for tissue or cell staining trans isomerization of proline imidic peptide bonds in 1:200. oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) Note: Optimal concentrations and conditions for each domain as well as an RNA-binding domain. It was shown to application should be determined by the user. possess PPIase and protein folding activities and also exhibit Precautions and Disclaimer RNA-binding activity. Three alternatively spliced transcript This product is for R&D use only, not for drug, household, or variants encoding distinct isoforms have been observed. other uses. Due to the sodium azide content a material NCBI Accession number: NP_006103.1 safety data sheet (MSDS) for this product has been sent to Swiss Prot Accession number: Q5TGA2 the attention of the safety officer of your institution.
[Show full text]
Maternal Obesity Programs Mitochondrial and Lipid Metabolism Gene Expression in Infant Umbilical Vein Endothelial Cells
International Journal of Obesity (2016), 1–8 © 2016 Macmillan Publishers Limited, part of Springer Nature. All rights reserved 0307-0565/16 www.nature.com/ijo ORIGINAL ARTICLE Maternal obesity programs mitochondrial and lipid metabolism gene expression in infant umbilical vein endothelial cells SMR Costa1,2,3,4, E Isganaitis2,3,4, TJ Matthews2, K Hughes2, G Daher2, JM Dreyfuss2, GAP da Silva1 and M-E Patti2,3 BACKGROUND/OBJECTIVES: Maternal obesity increases risk for childhood obesity, but molecular mechanisms are not well understood. We hypothesized that primary umbilical vein endothelial cells (HUVEC) from infants of overweight and obese mothers would harbor transcriptional patterns reﬂecting offspring obesity risk. SUBJECTS/METHODS: In this observational cohort study, we recruited 13 lean (pre-pregnancy body mass index (BMI) o25.0 kg m − 2) and 24 overweight-obese (‘ov-ob’, BMI ⩾ 25.0 kg m − 2) women. We isolated primary HUVEC, and analyzed both gene expression (Primeview, Affymetrix) and cord blood levels of hormones and adipokines. RESULTS: A total of 142 transcripts were differentially expressed in HUVEC from infants of overweight-obese mothers (false discovery rate, FDRo0.05). Pathway analysis revealed that genes involved in mitochondrial and lipid metabolism were negatively correlated with maternal BMI (FDRo0.05). To test whether these transcriptomic patterns were associated with distinct nutrient exposures in the setting of maternal obesity, we analyzed the cord blood lipidome and noted signiﬁcant increases in the levels of total free fatty acids (lean: 95.5 ± 37.1 μgml− 1, ov-ob: 124.1 ± 46.0 μgml− 1, P = 0.049), palmitate (lean: 34.5 ± 12.7 μgml− 1, ov-ob: 46.3 ± 18.4 μgml− 1, P =0.03) and stearate (lean: 20.8 ± 8.2 μgml− 1, ov-ob: 29.7 ± 17.2 μgml− 1, P = 0.04), in infants of overweight-obese mothers.
[Show full text]
Lysosomal Activity Regulates Caenorhabditis Elegans Mitochondrial Dynamics Through Vitamin B12 Metabolism
Lysosomal activity regulates Caenorhabditis elegans mitochondrial dynamics through vitamin B12 metabolism Wei Weia,b and Gary Ruvkuna,b,1 aDepartment of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114; and bDepartment of Genetics, Harvard Medical School, Boston, MA 02115 Contributed by Gary Ruvkun, June 18, 2020 (sent for review April 27, 2020; reviewed by Min Han and Alexander van der Bliek) Mitochondrial fission and fusion are highly regulated by energy Caenorhabditis elegans DRP-1 (DRP, dynamin-related protein) is demand and physiological conditions to control the production, a cytosolic dynamin that mediates mitochondrial fission, during activity, and movement of these organelles. Mitochondria are which DRP-1 is recruited to the mitochondrial outer membrane arrayed in a periodic pattern in Caenorhabditis elegans muscle, but to form spirals that constrict and sever the organelle (4–6). Two this pattern is disrupted by mutations in the mitochondrial fission other C. elegans GTPases, FZO-1 (Mitofusion 1, or MFN1 in component dynamin DRP-1. Here we show that the dramatically mammals) and EAT-3 (Optic Atrophy 1, or OPA1 in mammals), disorganized mitochondria caused by a mitochondrial fission- mediate the opposite activity of the fission–fusion cycle of mi- defective dynamin mutation is strongly suppressed to a more pe- tochondria: fusion of mitochondrial outer and inner membranes, riodic pattern by a second mutation in lysosomal biogenesis or respectively. Other receptors and mediators have been identified acidification. Vitamin B12 is normally imported from the bacterial by genetic analysis in yeast of the pathways for mitochondrial diet via lysosomal degradation of B12-binding proteins and trans- fusion and fission, although many are not conserved in animals port of vitamin B12 to the mitochondrion and cytoplasm.
[Show full text]
Supplemental Information Supplemental Figures
Supplemental Information Supplemental Figures Fig S1. Workflow of defining FM-states of MCF7 following drug treatment. Fig S2. Differential FM-factors between drug-treated MCF7 samples and drug-free samples. X-axis represents the effect size of difference of each FM-factor between the drug-treated samples and the drug-free samples, see methods. The Y-axis represents the negative log10 transformed FDR value measured by Mann-Whitney rank test, followed by Benjamini-Hochberg adjustment. Blue color dots show the FM- factors with FDR < 1e-6 and effect size less than -0.2. Red color dots show the FM- factors with FDR < 1e-6 and effect size greater than 0.2. Fig S3. Consensus clustering of the relative functional module factors for MCF7 cell lines after drug treatment. A-C. Consensus matrix for the number of clusters k = 3, 4 or 5. D. Cumulative density function for the consensus values. E. Relative change in area under CDF curve with the increase of k. F. Tracking plot of samples with different cluster solutions. Figures are generated using ConsensusClusterPlus R package(Wilkerson and Hayes, 2010). Fig S4. The relative expression level of transcriptional factors that show difference among different states. Fig S5. Workflow for predicting targetable vulnerabilities using the cell states of MCF7 after drug treatment. Supplemental Tables Table S1. Functional modules selected in this study. KEGG Pathways Category Cellular community - eukaryotes Cellular Processes Transport and catabolism Cellular Processes Cell motility Cellular Processes Apoptosis
[Show full text]
Engineered Type 1 Regulatory T Cells Designed for Clinical Use Kill Primary
ARTICLE Acute Myeloid Leukemia Engineered type 1 regulatory T cells designed Ferrata Storti Foundation for clinical use kill primary pediatric acute myeloid leukemia cells Brandon Cieniewicz,1* Molly Javier Uyeda,1,2* Ping (Pauline) Chen,1 Ece Canan Sayitoglu,1 Jeffrey Mao-Hwa Liu,1 Grazia Andolfi,3 Katharine Greenthal,1 Alice Bertaina,1,4 Silvia Gregori,3 Rosa Bacchetta,1,4 Norman James Lacayo,1 Alma-Martina Cepika1,4# and Maria Grazia Roncarolo1,2,4# Haematologica 2021 Volume 106(10):2588-2597 1Department of Pediatrics, Division of Stem Cell Transplantation and Regenerative Medicine, Stanford School of Medicine, Stanford, CA, USA; 2Stanford Institute for Stem Cell Biology and Regenerative Medicine, Stanford School of Medicine, Stanford, CA, USA; 3San Raffaele Telethon Institute for Gene Therapy, Milan, Italy and 4Center for Definitive and Curative Medicine, Stanford School of Medicine, Stanford, CA, USA *BC and MJU contributed equally as co-first authors #AMC and MGR contributed equally as co-senior authors ABSTRACT ype 1 regulatory (Tr1) T cells induced by enforced expression of interleukin-10 (LV-10) are being developed as a novel treatment for Tchemotherapy-resistant myeloid leukemias. In vivo, LV-10 cells do not cause graft-versus-host disease while mediating graft-versus-leukemia effect against adult acute myeloid leukemia (AML). Since pediatric AML (pAML) and adult AML are different on a genetic and epigenetic level, we investigate herein whether LV-10 cells also efficiently kill pAML cells. We show that the majority of primary pAML are killed by LV-10 cells, with different levels of sensitivity to killing. Transcriptionally, pAML sensitive to LV-10 killing expressed a myeloid maturation signature.
[Show full text]
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.
[Show full text]