MCFD2 Antibody

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Catalog: OM213417 Scan to get more validated information MCFD2 Antibody Catalog: OM213417 100ug Product profile Product name MCFD2 Antibody Antibody Type Primary Antibodies Key Feature Clonality Polyclonal Isotype Ig Host Species Rabbit Tested Applications WB ,IHC ,FC Species Reactivity Human Concentration 1 mg/ml Purification Target Information Gene Synonyms SDNSF Alternative Names MCFD2; SDNSF; Multiple coagulation factor deficiency protein 2; Neural stem cell-derived neuronal surviv al protein Molecular Weight(MW) 16390 Da Function The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected pr oteins. Plays a role in the secretion of coagulation factors Tissue Specificity This MCFD2 antibody is generated from rabbits immunized with a recombinant protein from human MCF D2. Cellular Localization Endoplasmic reticulum-Golgi intermediate compartment. Endoplasmic reticulum. Golgi apparatus Database Links Entrez Gene 90411 Entrez Gene 90411 Application Application Western blot analysis of MCFD2 Antibody in MDA-MB231 cell line lysates (35ug/lane). MCFD2 (arrow) was detected using the purified Pab. Application Formalin-fixed and paraffin-embedded human skin reacted with MCFD2 Antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. Application MCFD2 Antibody flow cytometric analysis of MDA-MB231 cells (right histogram) compared to a negative control cell (left histogram).FITC-conjugated goat-anti- rabbit secondary antibodies were used for the analysis. Application Notes WB~~1:100~500 IHC~~1:50~100 FC~~1:10~50: Additional Information Form Liquid Storage Instructions For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles. Storage Buffer Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified thro ugh protein A column. Note The product is for research use only,not for use in diagnostic or therapeutic procedures. OmnimAbs.com [email protected] 506 N. GARFIELD AVE # 210 ALHAMBRA, CA 91801 This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Familial Multiple Coagulation Factor Deficiencies
Journal of Clinical Medicine Article Familial Multiple Coagulation Factor Deficiencies (FMCFDs) in a Large Cohort of Patients—A Single-Center Experience in Genetic Diagnosis Barbara Preisler 1,†, Behnaz Pezeshkpoor 1,† , Atanas Banchev 2 , Ronald Fischer 3, Barbara Zieger 4, Ute Scholz 5, Heiko Rühl 1, Bettina Kemkes-Matthes 6, Ursula Schmitt 7, Antje Redlich 8 , Sule Unal 9 , Hans-Jürgen Laws 10, Martin Olivieri 11 , Johannes Oldenburg 1 and Anna Pavlova 1,* 1 Institute of Experimental Hematology and Transfusion Medicine, University Clinic Bonn, 53127 Bonn, Germany; [email protected] (B.P.); [email protected] (B.P.); [email protected] (H.R.); [email protected] (J.O.) 2 Department of Paediatric Haematology and Oncology, University Hospital “Tzaritza Giovanna—ISUL”, 1527 Sofia, Bulgaria; [email protected] 3 Hemophilia Care Center, SRH Kurpfalzkrankenhaus Heidelberg, 69123 Heidelberg, Germany; ronald.fi[email protected] 4 Department of Pediatrics and Adolescent Medicine, University Medical Center–University of Freiburg, 79106 Freiburg, Germany; [email protected] 5 Center of Hemostasis, MVZ Labor Leipzig, 04289 Leipzig, Germany; [email protected] 6 Hemostasis Center, Justus Liebig University Giessen, 35392 Giessen, Germany; [email protected] 7 Center of Hemostasis Berlin, 10789 Berlin-Schöneberg, Germany; [email protected] 8 Pediatric Oncology Department, Otto von Guericke University Children’s Hospital Magdeburg, 39120 Magdeburg, Germany; [email protected] 9 Division of Pediatric Hematology Ankara, Hacettepe University, 06100 Ankara, Turkey; Citation: Preisler, B.; Pezeshkpoor, [email protected] B.; Banchev, A.; Fischer, R.; Zieger, B.; 10 Department of Pediatric Oncology, Hematology and Clinical Immunology, University of Duesseldorf, Scholz, U.; Rühl, H.; Kemkes-Matthes, 40225 Duesseldorf, Germany; [email protected] B.; Schmitt, U.; Redlich, A.; et al.
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Alterations of Genetic Variants and Transcriptomic Features of Response to Tamoxifen in the Breast Cancer Cell Line
Alterations of Genetic Variants and Transcriptomic Features of Response to Tamoxifen in the Breast Cancer Cell Line Mahnaz Nezamivand-Chegini Shiraz University Hamed Kharrati-Koopaee Shiraz University https://orcid.org/0000-0003-2345-6919 seyed taghi Heydari ( [email protected] ) Shiraz University of Medical Sciences https://orcid.org/0000-0001-7711-1137 Hasan Giahi Shiraz University Ali Dehshahri Shiraz University of Medical Sciences Mehdi Dianatpour Shiraz University of Medical Sciences Kamran Bagheri Lankarani Shiraz University of Medical Sciences Research Keywords: Tamoxifen, breast cancer, genetic variants, RNA-seq. Posted Date: August 17th, 2021 DOI: https://doi.org/10.21203/rs.3.rs-783422/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/33 Abstract Background Breast cancer is one of the most important causes of mortality in the world, and Tamoxifen therapy is known as a medication strategy for estrogen receptor-positive breast cancer. In current study, two hypotheses of Tamoxifen consumption in breast cancer cell line (MCF7) were investigated. First, the effect of Tamoxifen on genes expression prole at transcriptome level was evaluated between the control and treated samples. Second, due to the fact that Tamoxifen is known as a mutagenic factor, there may be an association between the alterations of genetic variants and Tamoxifen treatment, which can impact on the drug response. Methods In current study, the whole-transcriptome (RNA-seq) dataset of four investigations (19 samples) were derived from European Bioinformatics Institute (EBI). At transcriptome level, the effect of Tamoxifen was investigated on gene expression prole between control and treatment samples.
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Analysis of Newly Detected Mutations in the MCFD2 Gene Giving Rise to Combined Deficiency of Coagulation Factors V and VIII
Haemophilia (2011), 1–5 DOI: 10.1111/j.1365-2516.2011.02529.x ORIGINAL ARTICLE Analysis of newly detected mutations in the MCFD2 gene giving rise to combined deficiency of coagulation factors V and VIII H. ELMAHMOUDI,*1 E. WIGREN, 1 A. LAATIRI,à A. JLIZI,* A. ELGAAIED,* E. GOUIDER§ and Y. LINDQVISTà *Laboratory of Genetics, Immunology and Human Pathologies, Tunis, Tunisia; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden; àDepartment of Hematology, Fattouma Bourguiba Hospital, Monastir, Tunisia; and §Hemophilia Treatment Center, Aziza Othmana Hospital, Tunis, Tunisia Summary. Combined deficiency of coagulation factor V uncharged asparagine. To elucidate the structural effect (FV) and factor VIII (FVIII) (F5F8D) is a rare autosomal of this mutation, we performed circular dichroism (CD) recessive disorder characterized by mild-to-moderate analysis of secondary structure and stability. In addi- bleeding and reduction in FV and FVIII levels in plasma. tion, CD analysis was performed on two missense F5F8D is caused by mutations in one of two different mutations found in previously reported F5F8D patients. genes, LMAN1 and MCFD2, which encode proteins Our results show that all analysed mutant variants that form a complex involved in the transport of FV and give rise to destabilized proteins and highlight the FVIII from the endoplasmic reticulum to the Golgi importance of a structurally intact and functional apparatus. Here, we report the identification of a novel MCFD2 for the efficient secretion of coagulation factors mutation Asp89Asn in the MCFD2 gene in a Tunisian V and VIII. patient. In the encoded protein, this mutation causes substitution of a negatively charged aspartate, involved Keywords: circular dichroism, combined FV and FVIII in several structurally important interactions, to an deficiency, LMAN1, MCFD2, mutations excessive bleeding during or after trauma, surgery, or Introduction labour.
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Combined Factor V and Factor VIII Deficiency in a Thai Patient
Haemophilia (2005), 11, 280–284 DOI: 10.1111/j.1365-2516.2005.01092.x CASE REPORT Combined factor V and factor VIII deficiency in a Thai patient: a case report of genotype and phenotype characteristics N. SIRACHAINAN,* B. ZHANG, A. CHUANSUMRIT,* S. PIPE,à W. SASANAKUL§ and D. GINSBURG *Department of Pediatrics, Faculty of Medicine, Ramathibodi Hospital, Mahidol University, Bangkok, Thailand; Department of Human Genetics; àDepartment of Pediatrics, University of Michigan, Ann Arbor, MI, USA; and §Research Center, Faculty of Medicine, Ramathibodi Hospital, Mahidol University, Bangkok, Thailand Summary. A Thai woman, with no family history of VIII concentrate, fresh frozen plasma and antifibrin- bleeding disorders, presented with excessive bleeding olytic agent.Gene analysis of the proband identified after minor trauma and tooth extraction. The two LMAN1 gene mutations; one of which is 823-1 screening coagulogram revealed prolonged activated G fi C, a novel splice acceptor site mutation that is partial thromboplastin time and prothrombin time. inherited from her father, the other is 1366 C fi T, The specific-factor assay confirmed the diagnosis a nonsense mutation that is inherited from her of combined factor V and factor VIII deficiency mother. Thus, the compound heterozygote of these (F5F8D). Her plasma levels of factor V and factor two mutations in LMAN1 cause combined F5F8D. VIII were 10% and 12.5% respectively. The medi- cations and blood product treatment to prevent Keywords: bleeding, combined factor V and factor bleeding from invasive procedure included 1-deami- VIII deficiency, ER-Golgi intermediate compartment no-8-d-arginine vasopressin, cryoprecipitate, factor protein, LMAN1 and 30% and the successful treatments in order to Introduction prevent bleeding from surgery include administration Combined factor V and factor VIII deficiency of 1-deamino-8-d-arginine vasopressin (DDAVP) and (F5F8D) is a rare autosomal recessive bleeding plasma transfusion [7,8].
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A Peripheral Blood Gene Expression Signature to Diagnose Subclinical Acute Rejection
CLINICAL RESEARCH www.jasn.org A Peripheral Blood Gene Expression Signature to Diagnose Subclinical Acute Rejection Weijia Zhang,1 Zhengzi Yi,1 Karen L. Keung,2 Huimin Shang,3 Chengguo Wei,1 Paolo Cravedi,1 Zeguo Sun,1 Caixia Xi,1 Christopher Woytovich,1 Samira Farouk,1 Weiqing Huang,1 Khadija Banu,1 Lorenzo Gallon,4 Ciara N. Magee,5 Nader Najaﬁan,5 Milagros Samaniego,6 Arjang Djamali ,7 Stephen I. Alexander,2 Ivy A. Rosales,8 Rex Neal Smith,8 Jenny Xiang,3 Evelyne Lerut,9 Dirk Kuypers,10,11 Maarten Naesens ,10,11 Philip J. O’Connell,2 Robert Colvin,8 Madhav C. Menon,1 and Barbara Murphy1 Due to the number of contributing authors, the afﬁliations are listed at the end of this article. ABSTRACT Background In kidney transplant recipients, surveillance biopsies can reveal, despite stable graft function, histologic features of acute rejection and borderline changes that are associated with undesirable graft outcomes. Noninvasive biomarkers of subclinical acute rejection are needed to avoid the risks and costs associated with repeated biopsies. Methods We examined subclinical histologic and functional changes in kidney transplant recipients from the prospective Genomics of Chronic Allograft Rejection (GoCAR) study who underwent surveillance biopsies over 2 years, identifying those with subclinical or borderline acute cellular rejection (ACR) at 3 months (ACR-3) post-transplant. We performed RNA sequencing on whole blood collected from 88 indi- viduals at the time of 3-month surveillance biopsy to identify transcripts associated with ACR-3, developed a novel sequencing-based targeted expression assay, and validated this gene signature in an independent cohort.
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Rabbit Anti-MCFD2 Antibody-SL18724R
SunLong Biotech Co.,LTD Tel: 0086-571- 56623320 Fax:0086-571- 56623318 E-mail:[email protected] www.sunlongbiotech.com Rabbit Anti-MCFD2 antibody SL18724R Product Name: MCFD2 Chinese Name: 多种凝血因子缺乏蛋白2抗体 1810021C21Rik; DKFZp686G21263; F5F8D; LMAN1IP; MCFD 2; Mcfd2; MCFD2_HUMAN; Multiple coagulation factor deficiency protein 2; Neural stem cell Alias: derived neuronal survival protein; Neural stem cell-derived neuronal survival protein; SDNSF. Organism Species: Rabbit Clonality: Polyclonal React Species: Human, ELISA=1:500-1000IHC-P=1:400-800IHC-F=1:400-800ICC=1:100-500IF=1:100- 500（Paraffin sections need antigen repair） Applications: not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. Molecular weight: 16kDa Cellular localization: cytoplasmic Form: Lyophilized or Liquid Concentration: 1mg/ml immunogen: KLHwww.sunlongbiotech.com conjugated synthetic peptide derived from human MCFD2:1-100/146 Lsotype: IgG Purification: affinity purified by Protein A Storage Buffer: 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year Storage: when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. PubMed: PubMed This gene encodes a soluble luminal protein with two calmodulin-like EF-hand motifs at its C-terminus. This protein forms a complex with LAMN1 (lectin mannose binding Product Detail: protein 1; also known as ERGIC-53) that facilitates the transport of coagulation factors V (FV) and VIII (FVIII) from the endoplasmic reticulum to the Golgi apparatus via an endoplasmic reticulum Golgi intermediate compartment (ERGIC).
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Molecular Targeting and Enhancing Anticancer Efficacy of Oncolytic HSV-1 to Midkine Expressing Tumors
University of Cincinnati Date: 12/20/2010 I, Arturo R Maldonado , hereby submit this original work as part of the requirements for the degree of Doctor of Philosophy in Developmental Biology. It is entitled: Molecular Targeting and Enhancing Anticancer Efficacy of Oncolytic HSV-1 to Midkine Expressing Tumors Student's name: Arturo R Maldonado This work and its defense approved by: Committee chair: Jeffrey Whitsett Committee member: Timothy Crombleholme, MD Committee member: Dan Wiginton, PhD Committee member: Rhonda Cardin, PhD Committee member: Tim Cripe 1297 Last Printed:1/11/2011 Document Of Defense Form Molecular Targeting and Enhancing Anticancer Efficacy of Oncolytic HSV-1 to Midkine Expressing Tumors A dissertation submitted to the Graduate School of the University of Cincinnati College of Medicine in partial fulfillment of the requirements for the degree of DOCTORATE OF PHILOSOPHY (PH.D.) in the Division of Molecular & Developmental Biology 2010 By Arturo Rafael Maldonado B.A., University of Miami, Coral Gables, Florida June 1993 M.D., New Jersey Medical School, Newark, New Jersey June 1999 Committee Chair: Jeffrey A. Whitsett, M.D. Advisor: Timothy M. Crombleholme, M.D. Timothy P. Cripe, M.D. Ph.D. Dan Wiginton, Ph.D. Rhonda D. Cardin, Ph.D. ABSTRACT Since 1999, cancer has surpassed heart disease as the number one cause of death in the US for people under the age of 85. Malignant Peripheral Nerve Sheath Tumor (MPNST), a common malignancy in patients with Neurofibromatosis, and colorectal cancer are midkine- producing tumors with high mortality rates. In vitro and preclinical xenograft models of MPNST were utilized in this dissertation to study the role of midkine (MDK), a tumor-specific gene over- expressed in these tumors and to test the efficacy of a MDK-transcriptionally targeted oncolytic HSV-1 (oHSV).
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Content Based Search in Gene Expression Databases and a Meta-Analysis of Host Responses to Infection
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Genotypes of Patients with Combined Factor V and VIII Deficiency
Genotypes of patients with combined factor V and VIII deficiency Gene Mutation Location Type Genotype Origin comments Reference LMAN1 Met1Thr* Exon 1 Initiation Hom Italy 1,2,3,4,5 codon LMAN1 nt 23 del G Exon 1 Frameshift Hom Iran 2 LMAN1 nt 31 del G Exon 1 Frameshift Hom Algeria 2 LMAN1 nt 89 ins G* Exon 1 Frameshift Hom Middle Eastern Founder 1,2,5,6,7 Jewish effect LMAN1 nt 89 ins G* Exon 1 Frameshift Hom Iran 2 LMAN1 nt 89 ins G* Exon 1 Frameshift Comp het Iran 2 nt 912 ins A* Exon 8 Frameshift LMAN1 Trp67Ser Exon 1 Missense Hom Japan 8 LMAN1 Gly114stop Exon 2 Nonsense Hom India 9 LMAN1 nt 422 del C Exon 3 Frameshift Comp het Japan 1 Undefined LMAN1 IVS4+17 del T Exon 4 Frameshift Comp het Turkey 10 Arg202stop* Exon 5 Missense LMAN1 Arg202stop* Exon 5 Nonsense Hom Japan 1,11 LMAN1 Arg202stop* Exon 5 Nonsense Hom Iran 2 LMAN1 Arg202stop* Exon 5 Nonsense Hom Tunis 12 LMAN1 IVS5+1G>T Intron 5 Splicing Hom Italy 2 LMAN1 nt 720 del 16bp Exon 6 Frameshift Hom Venezuela 1 LMAN1 nt 781 del T Exon 7 Frameshift Hom Austria 3 LMAN1 nt 795 del C Exon 7 Frameshift Hom Turkey 5 LMAN1 nt 813 del 72 bp Exon 7 Frameshift Hom India 13 LMAN1 nt 822 G>A* Exon 7 Splicing Hom Iran 2 LMAN1 IVS7+1 G>A Intron 7 Splicing Hom Belgium 3 LMAN1 IVS7+33 ins GGTT Intron 7 Splicing Comp het USA Skipping 3 Undefined exon 8 LMAN1 IVS7-1 G>C Intron 7 Splicing Comp het Thailand 14 Arg456stop* Exon 11 Nonsense LMAN1 nt 841 del A Exon 8 Frameshift Hom Poland 3 LMAN1 Lys302stop* Exon 8 Nonsense Hom Pakistan 2 LMAN1 Lys302stop* Exon 8 Nonsense Hom France 1 LMAN1 nt 912
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Familial Multiple Coagulation Factor Deficiencies
Journal of Thrombosis and Haemostasis, 2: 1564–1572 REVIEW ARTICLE Familial multiple coagulation factor deficiencies: new biologic insight from rare genetic bleeding disorders B. ZHANG andD. GINSBURG Departments of Internal Medicine and Human Genetics and the Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, USA To cite this article: Zhang B, Ginsburg D. Familial multiple coagulation factor deficiencies: new biologic insight from rare genetic bleeding disorders. J Thromb Haemost 2004; 2: 1564–72. transport and vitamin K metabolism, respectively. Little is Summary. Combined deficiency of factor (F)V and FVIII known about other types of multiple coagulation factor (F5F8D) and combined deficiency of vitamin K-dependent deficiencies, as only isolated case reports are available. clotting factors (VKCFD) comprise the vast majority of reported cases of familial multiple coagulation factor deficien- cies. Recently, significant progress has been made in under- Combined deficiency of FV and FVIII (F5F8D) standing the molecular mechanisms underlying these disorders. F5F8D is caused by mutations in two different genes (LMAN1 Biosynthesis of FV and FVIII and MCFD2) that encode components of a stable protein Hemostasis is mediated by the regulated and sequential complex. This complex is localized to the secretory pathway of activation of serine proteases in the coagulation cascade. FV the cell and likely functions in transporting newly synthesized and FVIII are two large plasma glycoproteins that function as FV and FVIII, and perhaps other proteins, from the ER to the essential cofactors for the proteolytic activation of prothrombin Golgi. VKCFD is either caused by mutations in the and FX, respectively. FV is synthesized primarily in hepatocytes c-carboxylase gene or in a recently identified gene encoding and megakaryocytes and is found in the plasma and a granules the vitamin K epoxide reductase.
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Crystal Structure of the LMAN1-CRD/MCFD2 Transport Receptor Complex Provides Insight Into Combined Deficiency of Factor V and Factor VIII
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 584 (2010) 878–882 journal homepage: www.FEBSLetters.org Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII Edvard Wigren, Jean-Marie Bourhis 1, Inari Kursula 2, Jodie E. Guy, Ylva Lindqvist * Dept. of Medical Biochemistry and Biophysics, Karolinska Institutet, 17177 Stockholm, Sweden article info abstract Article history: LMAN1 is a glycoprotein receptor, mediating transfer from the ER to the ER–Golgi intermediate Received 12 January 2010 compartment. Together with the co-receptor MCFD2, it transports coagulation factors V and VIII. Revised 29 January 2010 Mutations in LMAN1 and MCFD2 can cause combined deficiency of factors V and VIII (F5F8D). We Accepted 1 February 2010 present the crystal structure of the LMAN1/MCFD2 complex and relate it to patient mutations. Cir- Available online 9 February 2010 cular dichroism data show that the majority of the substitution mutations give rise to a disordered Edited by Kaspar Locher or severely destabilized MCFD2 protein. The few stable mutation variants are found in the binding surface of the complex leading to impaired LMAN1 binding and F5F8D. Keywords: Glycoprotein transport Structured summary: ER quality control MINT-7557086: lman1 (uniprotkb:P49257) and mcfd2 (uniprotkb:Q8NI22) bind (MI:0407) by X-ray crys- Protein complex tallography (MI:0114) Crystal structure ERGIC-53 Ó 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. 1. Introduction and FVIII e.g.
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Combined Deficiency of Factor V and Factor VIII Is Due to Mutations In
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2 Bin Zhang, Beth McGee, Jennifer S. Yamaoka, Hugo Guglielmone, Katharine A. Downes, Salvador Minoldo, Gustavo Jarchum, Flora Peyvandi, Norma B. de Bosch, Arlette Ruiz-Saez, Bernard Chatelain, Marian Olpinski, Paula Bockenstedt, Wolfgang Sperl, Randal J. Kaufman, William C. Nichols, Edward G. D. Tuddenham, and David Ginsburg Mutations in LMAN1 (ERGIC-53) or MCFD2 no LMAN1 mRNA accumulation. Com- F5F8D. Immunoprecipitation and West- cause combined deficiency of factor V bined with our previous reports, we have ern blot analysis detected a low level of and factor VIII (F5F8D). LMAN1 and identified LMAN1 or MCFD2 mutations as LMAN1-MCFD2 complex in lymphoblasts MCFD2 form a protein complex that func- the causes of F5F8D in 71 of 76 families. derived from patients with missense mu- tions as a cargo receptor ferrying FV and Among the 5 families in which no muta- tations in LMAN1 (C475R) or MCFD2 Downloaded from https://ashpublications.org/blood/article-pdf/107/5/1903/469004/zh800506001903.pdf by guest on 10 February 2020 FVIII from the endoplasmic reticulum to tions were identified, 3 were due to misdi- (I136T), suggesting that complete loss of the Golgi. In this study, we analyzed 10 agnosis, with the remaining 2 likely carry- the complex may not be required for previously reported and 10 new F5F8D ing LMAN1 or MCFD2 mutations that were clinically significant reduction in FV and families. Mutations in the LMAN1 or missed by direct sequencing. Our results FVIII.
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