The Role of Small In-Frame Insertions/Deletions in Inherited Eye
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Retinal Dystrophy Panel Plus
ANALYSIS REPORT Patient: Test, Test 1; DoB: 1989-Apr-10; Order ID: 54324 SUMMARY DIAGNOSTIC FINDING Retinal Dystrophy Panel Plus PATIENT INFORMATION NAME DOB SSN AGE GENDER ORDER ID Test, test1 1989-Apr-10 10041989-xxxx 28 Male 54324 REFERRING HEALTHCARE PROFESSIONAL NAME HOSPITAL Anna Smith Test hospital SUMMARY OF CLINICAL HISTORY Patient is a 28-year-old male with VA 20/40 OD, 20/50 OS, constricted visual fields, non-detectable rod ffERG, and a family history consistent with X-linked retinitis pigmentosa. SEQUENCE ANALYSIS RESULTS GENE NOMENCLATURE INHERITANCE ZYGOSITY CLASSIFICATION RPGR c.2655_2656del, p.(Glu886Glyfs*192) X-linked HEM LIKELY PATHOGENIC DEL/DUP (CNV) ANALYSIS RESULTS Del/Dup (CNV) analysis did not detect any known disease-causing copy number variation or novel or rare deletion/duplication that was considered deleterious. CONCLUSION We classify the identifiedRPGR c.2655_2656del, p.(Glu886Glyfs*192) as likely pathogenic and the probable cause for the patient’s disease, considering the current evidence of the variant (established association between the gene and the patient’s phenotype, rarity in control populations, identification of the variant in an individual with the same phenotype, and mutation type: frameshift). However, additional information is still needed to confirm the pathogenicity of the variant, which could allow independent risk stratification based on this mutation. Genetic counseling and family member testing is recommended. Disease caused by RPGR mutations is inherited in an X-linked manner. We recommend carrier testing of the mother. If the mother is a carrier, then each offspring has a 50% chance of inheriting the mutation. Disease caused byRPGR mutations is inherited in an X-linked manner, and thus each daughter of an affected male will inherit the mutation, while sons will remain unaffected. -
Building the Vertebrate Codex Using the Gene Breaking Protein Trap Library
Genetics, Development and Cell Biology Publications Genetics, Development and Cell Biology 2020 Building the vertebrate codex using the gene breaking protein trap library Noriko Ichino Mayo Clinic Gaurav K. Varshney National Institutes of Health Ying Wang Iowa State University Hsin-kai Liao Iowa State University Maura McGrail Iowa State University, [email protected] See next page for additional authors Follow this and additional works at: https://lib.dr.iastate.edu/gdcb_las_pubs Part of the Molecular Genetics Commons, and the Research Methods in Life Sciences Commons The complete bibliographic information for this item can be found at https://lib.dr.iastate.edu/ gdcb_las_pubs/261. For information on how to cite this item, please visit http://lib.dr.iastate.edu/howtocite.html. This Article is brought to you for free and open access by the Genetics, Development and Cell Biology at Iowa State University Digital Repository. It has been accepted for inclusion in Genetics, Development and Cell Biology Publications by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Building the vertebrate codex using the gene breaking protein trap library Abstract One key bottleneck in understanding the human genome is the relative under-characterization of 90% of protein coding regions. We report a collection of 1200 transgenic zebrafish strains made with the gene- break transposon (GBT) protein trap to simultaneously report and reversibly knockdown the tagged genes. Protein trap-associated mRFP expression shows previously undocumented expression of 35% and 90% of cloned genes at 2 and 4 days post-fertilization, respectively. Further, investigated alleles regularly show 99% gene-specific mRNA knockdown. -
RP2 Antibody / XRP2 (RQ4671)
RP2 Antibody / XRP2 (RQ4671) Catalog No. Formulation Size RQ4671 0.5mg/ml if reconstituted with 0.2ml sterile DI water 100 ug Bulk quote request Availability 1-3 business days Species Reactivity Human, Mouse, Rat Format Antigen affinity purified Clonality Polyclonal (rabbit origin) Isotype Rabbit IgG Purity Antigen affinity purified Buffer Lyophilized from 1X PBS with 2% Trehalose and 0.025% sodium azide UniProt O75695 Applications Western blot : 0.5-1ug/ml Immunohistochemistry (FFPE) : 1-2ug/ml Immunofluorescence : 2-4ug/ml Flow cytometry : 1-3ug/million cells Direct ELISA : 0.1-0.5ug/ml (human recombinant protein) Limitations This RP2 antibody is available for research use only. Western blot testing of 1) human placenta, 2) human SGC-7901, 3) rat lung and 4) mouse lung lysate with RP2 antibody at 0.5ug/ml. Predicted molecular weight ~40 kDa. IHC staining of FFPE human placenta with RP2 antibody at 1ug/ml. HIER: boil tissue sections in pH6, 10mM citrate buffer, for 10-20 min followed by cooling at RT for 20 min. IHC staining of FFPE human placenta with RP2 antibody at 1ug/ml. HIER: boil tissue sections in pH6, 10mM citrate buffer, for 10-20 min followed by cooling at RT for 20 min. IHC staining of FFPE human lung cancer with RP2 antibody at 1ug/ml. HIER: boil tissue sections in pH6, 10mM citrate buffer, for 10-20 min followed by cooling at RT for 20 min. IHC staining of FFPE human breast cancer with RP2 antibody at 1ug/ml. HIER: boil tissue sections in pH6, 10mM citrate buffer, for 10-20 min followed by cooling at RT for 20 min. -
Pigmentosa in a Large Kindred
J Med Genet: first published as 10.1136/jmg.28.7.453 on 1 July 1991. Downloaded from I Med Genet 1991; 28: 453-457 453 Genetic localisation of the RP2 type of X linked retinitis pigmentosa in a large kindred A F Wright, SS Bhattacharya, M A Aldred, M Jay, A D Carothers, N S T Thomas, A C Bird, B Jay, H J Evans Abstract and usually loss of central vision before the fourth Genetic linkage and deletion studies have led to the decade. At least 14 to 15% of families and 15 to 28% of proposal that there are at least two loci on the X retinitis pigmentosa patients in the UK have the X chromosome which are responsible for X linked linked disorder' 2 so that the population prevalence is retinitis pigmentosa (XLRP). One locus (RP3) has in the region of 1 in 10 000 to 30 000. been closely defined by genetic linkage and deletion XLRP was first mapped to the proximal short arm analyses and localised to the region between the of the X chromosome by genetic linkage to DXS7, ornithine transcarbamylase (OTC) and chronic localised to Xpl l.-pll .3.3 Subsequent linkage granulomatous disease (CYBB) loci in Xp2l.1- studies have supported locations both proximal49 and pII.4. The other locus (RP2) has been assigned by distal'o'3 to the DXS7 locus. The situation was linkage analysis alone to region Xpll.4-pll.2, but clarified by a heterogeneity analysis of 62 XLRP its localisation is less weli defined. The results of a kindreds from nine centres, in which it was shown multipoint linkage analysis of a single large XLRP that the overall likelihood was 6-4x 109:1 in favour of kindred using eight informative loci provide further two loci versus a single XLRP locus. -
Molecular Effects of Isoflavone Supplementation Human Intervention Studies and Quantitative Models for Risk Assessment
Molecular effects of isoflavone supplementation Human intervention studies and quantitative models for risk assessment Vera van der Velpen Thesis committee Promotors Prof. Dr Pieter van ‘t Veer Professor of Nutritional Epidemiology Wageningen University Prof. Dr Evert G. Schouten Emeritus Professor of Epidemiology and Prevention Wageningen University Co-promotors Dr Anouk Geelen Assistant professor, Division of Human Nutrition Wageningen University Dr Lydia A. Afman Assistant professor, Division of Human Nutrition Wageningen University Other members Prof. Dr Jaap Keijer, Wageningen University Dr Hubert P.J.M. Noteborn, Netherlands Food en Consumer Product Safety Authority Prof. Dr Yvonne T. van der Schouw, UMC Utrecht Dr Wendy L. Hall, King’s College London This research was conducted under the auspices of the Graduate School VLAG (Advanced studies in Food Technology, Agrobiotechnology, Nutrition and Health Sciences). Molecular effects of isoflavone supplementation Human intervention studies and quantitative models for risk assessment Vera van der Velpen Thesis submitted in fulfilment of the requirements for the degree of doctor at Wageningen University by the authority of the Rector Magnificus Prof. Dr M.J. Kropff, in the presence of the Thesis Committee appointed by the Academic Board to be defended in public on Friday 20 June 2014 at 13.30 p.m. in the Aula. Vera van der Velpen Molecular effects of isoflavone supplementation: Human intervention studies and quantitative models for risk assessment 154 pages PhD thesis, Wageningen University, Wageningen, NL (2014) With references, with summaries in Dutch and English ISBN: 978-94-6173-952-0 ABSTRact Background: Risk assessment can potentially be improved by closely linked experiments in the disciplines of epidemiology and toxicology. -
Null Mutation of the Fascin2 Gene by TALEN Leading to Progressive Hearing Loss and Retinal Degeneration in C57BL/6J Mice
G3: Genes|Genomes|Genetics Early Online, published on August 6, 2018 as doi:10.1534/g3.118.200405 Null mutation of the Fascin2 gene by TALEN leading to progressive hearing loss and retinal degeneration in C57BL/6J mice Xiang Liu1,3,§, Mengmeng Zhao1,2,§, Yi Xie1,2, §, Ping Li1, Oumei Wang1 , Bingxin Zhou1,2, Linlin Yang1,4, Yao Nie1, Lin Cheng1, Xicheng Song1,5, Changzhu Jin1,3,**, Fengchan Han1,2,* 1Key Laboratory for Genetic Hearing Disorders in Shandong, Binzhou Medical University, 346 Guanhai Road, Yantai264003, Shandong, P. R. China 2Department of Biochemistry and Molecular Biology, Binzhou Medical University, 346 Guanhai Road, Yantai264003, Shandong, P. R. China 3Department of Human Anatomy and Histology and Embryology, Binzhou Medical University, 346 Guanhai Road, Yantai264003, Shandong, P. R. China 4Department of Otorhinolaryngology-Head and Neck Surgery, Yuhuangding Hospital, 20 East Yuhuangding Road, Yantai 264000, Shandong, P.R .China § These authors contribute equally *The First Corresponding Author: [email protected] **The Second Corresponding Author: [email protected] Key Laboratory for Genetic Hearing Disorders in Shandong, Department of Biochemistry and Molecular Biology, Binzhou Medical University, 346 Guanhai Road, Yantai264003, Shandong, P. R. China © The Author(s) 2013. Published by the Genetics Society of America. Abstract Fascin2 (FSCN2) is an actin cross-linking protein that is mainly localized in retinas and in the stereocilia of hair cells. Earlier studies showed that a deletion mutation in human FASCIN2 (FSCN2) gene could cause autosomal dominant retinitis pigmentosa. Recent studies have indicated that a missense mutation in mouse Fscn2 gene (R109H) can contribute to the early onset of hearing loss in DBA/2J mice. -
Fascin (55Kd Actin-Bundling Protein, Singed-Like Protein, P55)
Fascin (55kD actin-bundling protein, Singed-like protein, p55) Catalog number 144510 Supplier United States Biological Fascin is a actin cross-linking protein.The Fascin gene contains 5 exons and spans 7 kb. It is a 54-58 kilodalton monomeric actin filament bundling protein originally isolated from sea urchin egg but also found in Drosophila and vertebrates, including humans. Fascin (from the Latin for bundle) is spaced at 11 nanometre intervals along the filament. The bundles in cross section are seen to be hexagonally packed, and the longitudinal spacing is compatible with a model where fascin cross-links at alternating 4 and 5 actins. It is calcium insensitive and monomeric. Fascin binds beta-catenin, and colocalizes with it at the leading edges and borders of epithelial and endothelial cells. The role of Fascin in regulating cytoskeletal structures for the maintenance of cell adhesion, coordinating motility and invasion through interactions with signalling pathways is an active area of research especially from the cancer biology perspective. Abnormal fascin expression or function has been implicated in breast cancer, colon cancer, esophageal squamous cell carcinoma, gallbladder cancer and prostate cancer. UniProt Number Q16658 Gene ID FSCN1 Applications Suitable for use in Western Blot. Recommended Dilution Optimal dilutions to be determined by the researcher. Storage and Handling Store at -20˚C for one year. After reconstitution, store at 4˚C for one month. Can also be aliquoted and stored frozen at -20˚C for long term. Avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. -
RP2 Phenotype and Pathogenetic Correlations in X-Linked Retinitis Pigmentosa
OPHTHALMIC MOLECULAR GENETICS SECTION EDITOR: JANEY L. WIGGS, MD, PhD RP2 Phenotype and Pathogenetic Correlations in X-Linked Retinitis Pigmentosa Thiran Jayasundera, MD; Kari E. H. Branham, MS; Mohammad Othman, PhD; William R. Rhoades, BS; Athanasios J. Karoukis, BS; Hemant Khanna, PhD; Anand Swaroop, PhD; John R. Heckenlively, MD Objectives: To assess the phenotype of patients with function. All 3 female carriers had macular atrophy in 1 X-linked retinitis pigmentosa (XLRP) with RP2 muta- or both eyes and were myopic (mean, −6.23 D). All 9 non- tions and to correlate the findings with their genotype. sense and frameshift and 5 of 7 missense mutations (71%) resulted in severe clinical presentations. Methods: Six hundred eleven patients with RP were screened for RP2 mutations. From this screen, 18 pa- Conclusions: Screening of the RP2 gene should be pri- tients with RP2 mutations were evaluated clinically with oritized in patients younger than 16 years characterized standardized electroretinography, Goldmann visual fields, by X-linked inheritance, decreased best-corrected vi- and ocular examinations. In addition, 7 well-docu- sual acuity (eg, Ͼ20/40), high myopia, and early-onset mented cases from the literature were used to augment macular atrophy. Patients exhibiting a choroideremia- genotype-phenotype correlations. like fundus without choroideremia gene mutations should also be screened for RP2 mutations. Results: Of 11 boys younger than 12 years, 10 (91%) had macular involvement and 9 (82%) had best- Clinical Relevance: An identifiable phenotype for corrected visual acuity worse than 20/50. Two boys from RP2-XLRP aids in clinical diagnosis and targeted genetic different families (aged 8 and 12 years) displayed a cho- roideremia-like fundus, and 9 boys (82%) were myopic screening. -
Fascin 2 (FSCN2) Goat Polyclonal Antibody – AP31070PU-N | Origene
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for AP31070PU-N Fascin 2 (FSCN2) Goat Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: ELISA, IHC Recommended Dilution: Peptide ELISA: Detection Limit: 1/64000. Western Blot: Preliminary experiments gave bands at approx 75kDa and 22kDa in Mouse Eye lysates after 0.05µg/ml antibody staining. Please note that currently we cannot find an explanation in the literature for the bands we observe given the calculated size of 57.4kDa according to NP_001070650.1 and 55.1kDa according to NP_036550.1. Both detected bands were successfully blocked by incubation with the immunizing peptide (and BLAST results with the immunizing peptide sequence did not identify any other proteins to explain the additional bands). Immunohistochemistry: This product was successfully used on Sections of Mouse cochlea as descibed in Reference 1. Reactivity: Canine, Human, Mouse, Rat Host: Goat Clonality: Polyclonal Immunogen: Peptide with sequence from the internal region of the protein sequence according to NP_001070650.1; NP_036550.1. Specificity: This antibody is expected to recognize both reported isoforms (NP_001070650.1 and NP_036550.1). Formulation: Tris saline, pH~7.3 containing 0.02% Sodium Azide as preservative and 0.5% BSA as stabilizer State: Aff - Purified State: Liquid purified Ig fraction Concentration: lot specific Purification: Affinity Chromatgraphy Conjugation: Unconjugated Storage: Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. -
Identification of the Fatty Acid Synthase Interaction Network Via Itraq-Based Proteomics Indicates the Potential Molecular Mecha
Huang et al. Cancer Cell Int (2020) 20:332 https://doi.org/10.1186/s12935-020-01409-2 Cancer Cell International PRIMARY RESEARCH Open Access Identifcation of the fatty acid synthase interaction network via iTRAQ-based proteomics indicates the potential molecular mechanisms of liver cancer metastasis Juan Huang1, Yao Tang1, Xiaoqin Zou1, Yi Lu1, Sha She1, Wenyue Zhang1, Hong Ren1, Yixuan Yang1,2* and Huaidong Hu1,2* Abstract Background: Fatty acid synthase (FASN) is highly expressed in various types of cancer and has an important role in carcinogenesis and metastasis. To clarify the mechanisms of FASN in liver cancer invasion and metastasis, the FASN protein interaction network in liver cancer was identifed by targeted proteomic analysis. Methods: Wound healing and Transwell assays was performed to observe the efect of FASN during migration and invasion in liver cancer. Isobaric tags for relative and absolute quantitation (iTRAQ)-based mass spectrometry were used to identify proteins interacting with FASN in HepG2 cells. Diferential expressed proteins were validated by co-immunoprecipitation, western blot analyses and confocal microscopy. Western blot and reverse transcription- quantitative polymerase chain reaction (RT-qPCR) were performed to demonstrate the mechanism of FASN regulating metastasis. Results: FASN knockdown inhibited migration and invasion of HepG2 and SMMC7721 cells. A total of, 79 proteins interacting with FASN were identifed. Additionally, gene ontology term enrichment analysis indicated that the majority of biological regulation and cellular processes that the FASN-interacting proteins were associated with. Co- precipitation and co-localization of FASN with fascin actin-bundling protein 1 (FSCN1), signal-induced proliferation- associated 1 (SIPA1), spectrin β, non-erythrocytic 1 (SPTBN1) and CD59 were evaluated. -
Reed-Sternberg Cell Marker)(Clone : FSCN1/417
9853 Pacific Heights Blvd. Suite D. San Diego, CA 92121, USA Tel: 858-263-4982 Email: [email protected] 36-1691: Monoclonal Antibody to Fascin-1 (Reed-Sternberg Cell Marker)(Clone : FSCN1/417) Clonality : Monoclonal Clone Name : FSCN1/417 Application : FACS,IF,WB,IHC Reactivity : Human Gene : FSCN1 Gene ID : 6624 Uniprot ID : Q16658 Format : Purified Alternative Name : FSCN1,FAN1,HSN,SNL Isotype : Mouse IgG2a Immunogen Information : Full length recombinant human FSCN1 protein Description Recognizes a protein of 55kDa, which is identified as fascin-1. Its actin binding ability is regulated by phosphorylation. Antibody to fascin-1 is a very sensitive marker for Reed-Sternberg cells and variants in nodular sclerosis, mixed cellularity, and lymphocyte depletion Hodgkin's disease. It is uniformly negative in lymphoid cells, plasma cells, and myeloid cells. Fascin-1 is also expressed in dendritic cells. This marker may be helpful to distinguish between Hodgkin lymphoma and non-Hodgkin lymphoma in difficult cases. Also, the lack of expression of fascin-1 in the neoplastic follicles in follicular lymphoma may be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased. Antibody to fascin-1 has been suggested as a prognostic marker in neuroendocrine neoplasms of the lung as well as in ovarian cancer. Fascin-1 expression may be induced by Epstein-Barr virus (EBV) infection of B cells with the possibility that viral induction of fascin in lymphoid or other cell types must also be considered in EBV-positive cases. Product Info Amount : 100 µg Purification : Affinity Chromatography 100 µg in 500 µl PBS containing 0.05% BSA and 0.05% sodium azide. -
Roles of Fascin Mrna Expression in Colorectal Cancer: Meta‑Analysis and Bioinformatics Analysis
MOLECULAR AND CLINICAL ONCOLOGY 13: 119-128, 2020 Roles of Fascin mRNA expression in colorectal cancer: Meta‑analysis and bioinformatics analysis SHUAI SHI, HUA-CHUAN ZHENG and ZHI-GANG ZHANG Department of Pathology, Cangzhou People's Hospital, Cangzhou, Hebei 061000, P.R. China Received July 4, 2019; Accepted April 22, 2020 DOI: 10.3892/mco.2020.2069 Abstract. Fascin (encoded by FSCN1) is a globular actin depth of invasion, microsatellite instability and low serum cross-linking protein that is required for the formation of carcinoembryonic antigen levels in colorectal cancer. Taken actin-based cell surface processes, which are critical for cell together, the results of the present study suggested that Fascin migration and cell-matrix adhesion. In the present study, a expression is a potential marker of tumorigenesis, aggressive- systematic meta-analysis and bioinformatics analysis was ness and poor prognosis in patients with colorectal cancer. used to identify clinicopathological or prognostic parameters in patients with colorectal cancer. A total of 17 articles were Introduction included in the present study obtained from PubMed, Web of Science, Wanfang data, SinoMed and CNKI databases. Fascin is a cytoskeletal protein, is one of the important Odd ratios (ORs) and the corresponding 95% confidence members of the Fascin family of proteins and is located on intervals (CIs) were used to estimate the prognostic signifi- chromosome 7q22 (1). An N-terminal serine participates cance of Fascin expression in patients with colorectal cancer, in actin binding, which is also the phosphorylation site of and the association between Fascin expression and clini- protein kinase C. The phosphorylation of this site regulates copathological factors.