FREM1 Blocking Peptide (CDBP5460) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use

Total Page：16

File Type：pdf, Size：1020Kb

FREM1 blocking peptide (CDBP5460) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description This gene encodes a basement membrane protein that may play a role in craniofacial and renal development. Mutations in this gene have been associated with bifid nose with or without anorectal and renal anomalies. Alternatively spliced transcript variants encoding different isoforms have been described. PubMed ID 19940113 describes one such variant that initiates transcription within a distinct, internal exon; the resulting shorter isoform (named Toll- like/interleukin-1 receptor regulator, TILRR) is suggested to be a co-receptor of the interleukin 1 receptor family and may regulate receptor function and Toll-like receptor/interleukin 1 receptor signal transduction, contributing to the control of inflammatory response activation. [provided by RefSeq, Apr 2011] Immunogen 15 amino acids near the carboxy terminus of human FRAM1. Nature Synthetic Expression System N/A Species Reactivity Mouse, human Conjugate Unconjugated Applications Used as a blocking peptide in immunoblotting applications. Procedure None Format Liquid Concentration 200 μg/mL Size 0.05mg Preservative None Storage -20°C ANTIGEN GENE INFORMATION Gene Name FREM1 FRAS1 related extracellular matrix 1 [ Homo sapiens (human) ] Official Symbol FREM1 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Synonyms FREM1; FRAS1 related extracellular matrix 1; BNAR; MOTA; TILRR; TRIGNO2; C9orf143; C9orf145; C9orf154; FRAS1-related extracellular matrix protein 1; extracellular matrix protein QBRICK Entrez Gene ID 158326 mRNA Refseq NM_001177704 Protein Refseq NP_001171175 UniProt ID Q5H8C1 Function carbohydrate binding; metal ion binding 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.

Copy Link

Recommended publications

Supplementary Table 3 Complete List of RNA-Sequencing Analysis of Gene Expression Changed by ≥ Tenfold Between Xenograft and Cells Cultured in 10%O2
Supplementary Table 3 Complete list of RNA-Sequencing analysis of gene expression changed by ≥ tenfold between xenograft and cells cultured in 10%O2 Expr Log2 Ratio Symbol Entrez Gene Name (culture/xenograft) -7.182 PGM5 phosphoglucomutase 5 -6.883 GPBAR1 G protein-coupled bile acid receptor 1 -6.683 CPVL carboxypeptidase, vitellogenic like -6.398 MTMR9LP myotubularin related protein 9-like, pseudogene -6.131 SCN7A sodium voltage-gated channel alpha subunit 7 -6.115 POPDC2 popeye domain containing 2 -6.014 LGI1 leucine rich glioma inactivated 1 -5.86 SCN1A sodium voltage-gated channel alpha subunit 1 -5.713 C6 complement C6 -5.365 ANGPTL1 angiopoietin like 1 -5.327 TNN tenascin N -5.228 DHRS2 dehydrogenase/reductase 2 leucine rich repeat and fibronectin type III domain -5.115 LRFN2 containing 2 -5.076 FOXO6 forkhead box O6 -5.035 ETNPPL ethanolamine-phosphate phospho-lyase -4.993 MYO15A myosin XVA -4.972 IGF1 insulin like growth factor 1 -4.956 DLG2 discs large MAGUK scaffold protein 2 -4.86 SCML4 sex comb on midleg like 4 (Drosophila) Src homology 2 domain containing transforming -4.816 SHD protein D -4.764 PLP1 proteolipid protein 1 -4.764 TSPAN32 tetraspanin 32 -4.713 N4BP3 NEDD4 binding protein 3 -4.705 MYOC myocilin -4.646 CLEC3B C-type lectin domain family 3 member B -4.646 C7 complement C7 -4.62 TGM2 transglutaminase 2 -4.562 COL9A1 collagen type IX alpha 1 chain -4.55 SOSTDC1 sclerostin domain containing 1 -4.55 OGN osteoglycin -4.505 DAPL1 death associated protein like 1 -4.491 C10orf105 chromosome 10 open reading frame 105 -4.491
[Show full text]
Human Lectins, Their Carbohydrate Affinities and Where to Find Them
biomolecules Review Human Lectins, Their Carbohydrate Affinities and Where to Review HumanFind Them Lectins, Their Carbohydrate Afﬁnities and Where to FindCláudia ThemD. Raposo 1,*, André B. Canelas 2 and M. Teresa Barros 1 1, 2 1 Cláudia D. Raposo * , Andr1 é LAQVB. Canelas‐Requimte,and Department M. Teresa of Chemistry, Barros NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829‐516 Caparica, Portugal; [email protected] 12 GlanbiaLAQV-Requimte,‐AgriChemWhey, Department Lisheen of Chemistry, Mine, Killoran, NOVA Moyne, School E41 of ScienceR622 Co. and Tipperary, Technology, Ireland; canelas‐ [email protected] NOVA de Lisboa, 2829-516 Caparica, Portugal; [email protected] 2* Correspondence:Glanbia-AgriChemWhey, [email protected]; Lisheen Mine, Tel.: Killoran, +351‐212948550 Moyne, E41 R622 Tipperary, Ireland; [email protected] * Correspondence: [email protected]; Tel.: +351-212948550 Abstract: Lectins are a class of proteins responsible for several biological roles such as cell‐cell in‐ Abstract:teractions,Lectins signaling are pathways, a class of and proteins several responsible innate immune for several responses biological against roles pathogens. such as Since cell-cell lec‐ interactions,tins are able signalingto bind to pathways, carbohydrates, and several they can innate be a immuneviable target responses for targeted against drug pathogens. delivery Since sys‐ lectinstems. In are fact, able several to bind lectins to carbohydrates, were approved they by canFood be and a viable Drug targetAdministration for targeted for drugthat purpose. delivery systems.Information In fact, about several specific lectins carbohydrate were approved recognition by Food by andlectin Drug receptors Administration was gathered for that herein, purpose. plus Informationthe specific organs about speciﬁc where those carbohydrate lectins can recognition be found by within lectin the receptors human was body.
[Show full text]
Duplication 9P and Their Implication to Phenotype
Guilherme et al. BMC Medical Genetics (2014) 15:142 DOI 10.1186/s12881-014-0142-1 RESEARCH ARTICLE Open Access Duplication 9p and their implication to phenotype Roberta Santos Guilherme1, Vera Ayres Meloni1, Ana Beatriz Alvarez Perez1, Ana Luiza Pilla1, Marco Antonio Paula de Ramos1, Anelisa Gollo Dantas1, Sylvia Satomi Takeno1, Leslie Domenici Kulikowski2 and Maria Isabel Melaragno1* Abstract Background: Trisomy 9p is one of the most common partial trisomies found in newborns. We report the clinical features and cytogenomic findings in five patients with different chromosome rearrangements resulting in complete 9p duplication, three of them involving 9p centromere alterations. Methods: The rearrangements in the patients were characterized by G-banding, SNP-array and fluorescent in situ hybridization (FISH) with different probes. Results: Two patients presented de novo dicentric chromosomes: der(9;15)t(9;15)(p11.2;p13) and der(9;21)t(9;21) (p13.1;p13.1). One patient presented two concomitant rearranged chromosomes: a der(12)t(9;12)(q21.13;p13.33) and an psu i(9)(p10) which showed FISH centromeric signal smaller than in the normal chromosome 9. Besides the duplication 9p24.3p13.1, array revealed a 7.3 Mb deletion in 9q13q21.13 in this patient. The break in the psu i(9) (p10) probably occurred in the centromere resulting in a smaller centromere and with part of the 9q translocated to the distal 12p with the deletion 9q occurring during this rearrangement. Two patients, brother and sister, present 9p duplication concomitant to 18p deletion due to an inherited der(18)t(9;18)(p11.2;p11.31)mat.
[Show full text]
FREM1 Sirna (M): Sc-75060
SANTA CRUZ BIOTECHNOLOGY, INC. FREM1 siRNA (m): sc-75060 BACKGROUND PRODUCT FREM1 (FRAS1 related extracellular matrix 1), also known as QBRICK or FREM1 siRNA (m) is a pool of 3 target-specific 19-25 nt siRNAs designed C9orf154, is a 2,179 amino acid protein that contains one C-type lectin to knock down gene expression. Each vial contains 3.3 nmol of lyophilized domain, one Calx-b domain and 12 CSPG repeats. Localized to the basement siRNA, sufficient for a 10 µM solution once resuspended using protocol membrane of embryonic epidermal cells and secreted into extracellular space, below. Suitable for 50-100 transfections. Also see FREM1 shRNA FREM1 functions as an extracellular matrix protein that is essential for epider- Plasmid (m): sc-75060-SH and FREM1 shRNA (m) Lentiviral Particles: mal adhesion during embryogenesis and may also participate in epidermal sc-75060-V as alternate gene silencing products. differentiation. FREM1 exists as multiple alternatively spliced isoforms and is For independent verification of FREM1 (m) gene silencing results, we also encoded by a gene which maps to human chromosome 9p22.3. Chromosome 9 provide the individual siRNA duplex components. Each is available as contains 145 million base pairs and comprises 4% of the human genome, 3.3 nmol of lyophilized siRNA. These include: sc-75060A, sc-75060B and encoding nearly 900 genes. Hereditary hemorrhagic telangiectasia, which is sc-75060C. characterized by harmful vascular defects, and familial dysautonomia, are both associated with chromosome 9. Notably, chromosome 9 encompasses STORAGE AND RESUSPENSION the largest interferon family gene cluster. Store lyophilized siRNA duplex at -20° C with desiccant.
[Show full text]
A Proposed Mouse Mutant Resequencing Initiative a Recommendation to Augment the Positional Cloning of Mouse Muta
A Proposed Mouse Mutant Resequencing Initiative A recommendation to augment the positional cloning of mouse mutations by resequencing of geneticallydefined critical regions at Genome Centers. The longterm goal of the human genome project (HGP) is to define and understand the functions of all human genes and their relationships to health and disease. The HGP has revolutionized genetic research, having yielded complete genome sequences, comprehensive polymorphic genetic marker sets, and other molecular reagents for humans, mice and many other experimental organisms. This has greatly simplified positional cloning of disease genes and genetic mapping of simple and complex traits. Concurrent efforts have identified thousands of expressed genes, and coupled with highthroughput gene expression and protein analysis technologies, we are in the powerful position of knowing the sequence identity of most genes, their expression patterns, the chromatin states around genes, and networks of interacting proteins. While these data are valuable for deducing or suggesting the roles of genes in development and disease, the in vivo functions of most mammalian genes remain unknown. And their characterization remains a formidable challenge. With the advent of RNAi technologies, it has been possible to qualitatively assay large sets of genes for particular functions in simple animals such as C. elegans. In mammals, such technologies are being applied to cultured cells, but this approach will not address genes that function in developmental processes or differentiated tissues for which there is no in vitro model. The task of elucidating the in vivo function of human genes in disease and development relies heavily upon utilization of the mouse, in which mutations can be created in various ways.
[Show full text]
SARS-Cov-2 3Clpro Whole Human Proteome Cleavage
bioRxiv preprint doi: https://doi.org/10.1101/2020.08.24.265645; this version posted December 21, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 1 SARS-CoV-2 3CLpro whole human proteome cleavage prediction and 2 enrichment/depletion analysis 3 Lucas Prescott 4 Correspondence: [email protected] 5 Keywords: SARS-CoV-2, COVID-19, coronavirus, protease, proteomics, 3CLpro, machine learning, neural 6 networks 7 8 Abstract 9 A novel coronavirus (SARS-CoV-2) has devastated the globe as a pandemic that has killed more 10 than 1,600,000 people. Widespread vaccination is still uncertain, so many scientific efforts have been 11 directed toward discovering antiviral treatments. Many drugs are being investigated to inhibit the 12 coronavirus main protease, 3CLpro, from cleaving its viral polyprotein, but few publications have 13 addressed this protease’s interactions with the host proteome or their probable contribution to 14 virulence. Too few host protein cleavages have been experimentally verified to fully understand 15 3CLpro’s global effects on relevant cellular pathways and tissues. Here, I set out to determine this 16 protease’s targets and corresponding potential drug targets. Using a neural network trained on 17 cleavages from 388 coronavirus proteomes with a Matthews correlation coefficient of 0.983, I predict 18 that a large proportion of the human proteome is vulnerable to 3CLpro, with 4,460 out of approximately 19 20,000 human proteins containing at least one putative cleavage site.
[Show full text]
Microarray Analysis of Iris Gene Expression in Mice with Mutations Influencing Pigmentation
Glaucoma Microarray Analysis of Iris Gene Expression in Mice with Mutations Influencing Pigmentation Colleen M. Trantow,1 Tryphena L. Cuffy,2 John H. Fingert,2,3 Markus H. Kuehn,2,3 and Michael G. Anderson1,2,3 PURPOSE. Several ocular diseases involve the iris, notably includ- lak syndrome, Chediak-Higashi syndrome, Horner’s syndrome, ing oculocutaneous albinism, pigment dispersion syndrome, Waardenburg syndrome, and Fuchs’ heterochromic iridocycli- and exfoliation syndrome. To screen for candidate genes that tis. In addition, other ocular diseases, such as pigment disper- may contribute to the pathogenesis of these diseases, genome- sion syndrome and exfoliation syndrome, involve disease-re- wide iris gene expression patterns were comparatively ana- lated morphologic changes to the pigmented tissues of the iris. lyzed from mouse models of these conditions. Each of these diseases involves strong hereditary links, but METHODS. Iris samples from albino mice with a Tyr mutation, much remains unknown concerning the underlying genetic pigment dispersion–prone mice with Tyrp1 and Gpnmb mu- pathways. In this study, we focused on three of these condi- tations, and mice resembling exfoliation syndrome with a Lyst tions: albinism, pigment dispersion syndrome, and exfoliation mutation were compared with samples from wild-type mice. syndrome. All mice were strain (C57BL/6J), age (60 days old), and sex In oculocutaneous albinism (OCA), there is reduced or (female) matched. Microarrays were used to compare tran- absent pigmentation of the skin, hair, and eyes. Decreased scriptional profiles, and differentially expressed transcripts melanin in the eyes can give rise to several ocular abnormali- were described by functional annotation clustering using ties, including foveal hypoplasia and decreased visual acuity; DAVID Bioinformatics Resources.
[Show full text]
Evidence for Additional FREM1 Heterogeneity in Manitoba Oculotrichoanal Syndrome
Molecular Vision 2012; 18:1301-1311 <http://www.molvis.org/molvis/v18/a137> © 2012 Molecular Vision Received 17 April 2012 | Accepted 24 May 2012 | Published 30 May 2012 Evidence for additional FREM1 heterogeneity in Manitoba oculotrichoanal syndrome Robertino Karlo Mateo,1 Royce Johnson,2 Ordan J. Lehmann1,2 1Department of Medical Genetics, University of Alberta, Edmonton, Canada; 2Department of Ophthalmology, University of Alberta, Edmonton, Canada Purpose: Manitoba Oculotrichoanal (MOTA) syndrome is an autosomal recessive disorder present in First Nations families that is characterized by ocular (cryptophthalmos), facial, and genital anomalies. At the commencement of this study, its genetic basis was undefined. Methods: Homozygosity analysis was employed to map the causative locus using DNA samples from four probands of Cree ancestry. After single nucleotide polymorphism (SNP) genotyping, data were analyzed and exported to PLINK to identify regions identical by descent (IBD) and common to the probands. Candidate genes within and adjacent to the IBD interval were sequenced to identify pathogenic variants, with analyses of potential deletions or duplications undertaken using the B-allele frequency and log2 ratio of SNP signal intensity. Results: Although no shared IBD region >1 Mb was evident on preliminary analysis, adjusting the criteria to permit the detection of smaller homozygous IBD regions revealed one 330 Kb segment on chromosome 9p22.3 present in all 4 probands. This interval comprising 152 SNPs, lies 16 Kb downstream of FRAS1-related extracellular matrix protein 1 (FREM1), and no copy number variations were detected either in the IBD region or FREM1. Subsequent sequencing of both genes in the IBD region, followed by FREM1, did not reveal any mutations.
[Show full text]
Comparative Study of Organoids from Patient-Derived Normal and Tumor Colon and Rectal Tissue
cancers Article Comparative Study of Organoids from Patient-Derived Normal and Tumor Colon and Rectal Tissue Alba Costales-Carrera 1,2,3 , Asunción Fernández-Barral 1,2,3 , Pilar Bustamante-Madrid 1,2,3 , Orlando Domínguez 4 , Laura Guerra-Pastrián 2,5 , Ramón Cantero 2,6 , Luis del Peso 1,7, 8 1,2,3, 1,2,3, , Aurora Burgos , Antonio Barbáchano y and Alberto Muñoz * y 1 Departamento de Biología del Cáncer, Instituto de Investigaciones Biomédicas “Alberto Sols”, Consejo Superior de Investigaciones Cientíﬁcas (CSIC)-Universidad Autónoma de Madrid (UAM), 28029 Madrid, Spain; [email protected] (A.C.-C.); [email protected] (A.F.-B.); [email protected] (P.B.-M.); [email protected] (L.d.P.); [email protected] (A.B.) 2 Instituto de Investigación del Hospital Universitario La Paz (IdiPAZ), 28029 Madrid, Spain; [email protected] (L.G.-P.); [email protected] (R.C.) 3 Centro de Investigaciones Biomédicas en Red-Cáncer (CIBERONC), 28029 Madrid, Spain 4 Unidad de Genómica, Centro Nacional de Investigaciones Oncológicas (CNIO), 28029 Madrid, Spain; [email protected] 5 Departamento de Patología, Hospital Universitario La Paz, 28029 Madrid, Spain 6 Unidad Colorrectal, Departamento de Cirugía, Hospital Universitario La Paz, 28029 Madrid, Spain 7 Centro de Investigaciones Biomédicas en Red-Enfermedades Respiratorias (CIBERES), 28029 Madrid, Spain 8 Unidad de Endoscopia, Departamento de Digestivo, Hospital Universitario La Paz, 28029 Madrid, Spain; [email protected] * Correspondence: [email protected] These authors contributed equally as Co-Last. y Received: 24 July 2020; Accepted: 13 August 2020; Published: 15 August 2020 Abstract: Colon and rectal tumors, often referred to as colorectal cancer, show diﬀerent gene expression patterns in studies that analyze whole tissue biopsies containing a mix of tumor and non-tumor cells.
[Show full text]
Supplemental Information
Supplementary Information Genome-wide association analyses of risk tolerance and risky behaviors in over one million individuals identify hundreds of loci and shared genetic influences Correspondence to: [email protected] or [email protected] TABLE OF CONTENTS 1 STUDY OVERVIEW ............................................................................................................. 4 1.1 STUDY MOTIVATION ........................................................................................................... 4 1.2 PHENOTYPE DEFINITIONS .................................................................................................... 4 2 GWAS, QUALITY CONTROL AND META-ANALYSIS ............................................. 10 2.1 OVERVIEW OF PRIMARY GWAS ....................................................................................... 10 2.2 GENOTYPING AND IMPUTATION ........................................................................................ 11 2.3 ASSOCIATION ANALYSES .................................................................................................. 11 2.4 MAIN REFERENCE PANEL .................................................................................................. 12 2.5 QUALITY CONTROL OF ALLELE-FREQUENCY DIFFERENCES BETWEEN THE UK BIOBANK GENOTYPING ARRAYS ................................................................................................................. 14 2.6 DESCRIPTION OF MAJOR STEPS IN QUALITY-CONTROL (QC) ANALYSES ...........................
[Show full text]
Heterozygous Mutations of FREM1 Are Associated with an Increased Risk of Isolated Metopic Craniosynostosis in Humans and Mice
Heterozygous Mutations of FREM1 Are Associated with an Increased Risk of Isolated Metopic Craniosynostosis in Humans and Mice Lisenka E. L. M. Vissers1., Timothy C. Cox2,3., A. Murat Maga2., Kieran M. Short4, Fenny Wiradjaja4, Irene M. Janssen1, Fernanda Jehee5, Debora Bertola5, Jia Liu6, Garima Yagnik6, Kiyotoshi Sekiguchi7, Daiji Kiyozumi7, Hans van Bokhoven1,8, Carlo Marcelis1, Michael L. Cunningham2, Peter J. Anderson9, Simeon A. Boyadjiev6, Maria Rita Passos-Bueno5, Joris A. Veltman1, Ian Smyth3,4, Michael F. Buckley1,10, Tony Roscioli1,11* 1 Department of Human Genetics, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands, 2 Division of Craniofacial Medicine, Department of Pediatrics, University of Washington, Seattle, Washington, United States of America, 3 Department of Anatomy and Developmental Biology, Monash University, Clayton, Australia, 4 Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia, 5 Centro de Estudos do Genoma Humano, Instituto de Biocieˆncias, Universidade de Sa˜o Paulo, Sa˜o Paulo, Brasil, 6 Section of Genetics, Department of Pediatrics, University of California Davis, Sacramento, California, United States of America, 7 Institute for Protein Research, Osaka University, Osaka, Japan, 8 Donders Institute for Brain, Imaging, and Cognition, Nijmegen, The Netherlands, 9 Australian Craniofacial Unit, Women and Children’s Hospital, Adelaide, Australia, 10 Department of Haematology and Genetics, South- Eastern Area Laboratory Services, Prince of Wales and Sydney Children’s Hospitals, Randwick, Australia, 11 Sydney South West Genetic Service, Royal Prince Alfred Hospital, Sydney University, Sydney, Australia Abstract The premature fusion of the paired frontal bones results in metopic craniosynostosis (MC) and gives rise to the clinical phenotype of trigonocephaly.
[Show full text]
Quantitative in Vivo Whole Genome Motility Screen Reveals Novel Therapeutic Targets to Block Cancer Metastasis
ARTICLE DOI: 10.1038/s41467-018-04743-2 OPEN Quantitative in vivo whole genome motility screen reveals novel therapeutic targets to block cancer metastasis Konstantin Stoletov1, Lian Willetts1, Robert J. Paproski1, David J. Bond1, Srijan Raha1, Juan Jovel2,3, Benjamin Adam4, Amy E. Robertson1, Francis Wong1, Emma Woolner1, Deborah L. Sosnowski1, Tarek A. Bismar5, Gane Ka-Shu Wong2,3,6, Andries Zijlstra 7 & John D. Lewis 1 1234567890():,; Metastasis is the most lethal aspect of cancer, yet current therapeutic strategies do not target its key rate-limiting steps. We have previously shown that the entry of cancer cells into the blood stream, or intravasation, is highly dependent upon in vivo cancer cell motility, making it an attractive therapeutic target. To systemically identify genes required for tumor cell motility in an in vivo tumor microenvironment, we established a novel quantitative in vivo screening platform based on intravital imaging of human cancer metastasis in ex ovo avian embryos. Utilizing this platform to screen a genome-wide shRNA library, we identiﬁed a panel of novel genes whose function is required for productive cancer cell motility in vivo, and whose expression is closely associated with metastatic risk in human cancers. The RNAi-mediated inhibition of these gene targets resulted in a nearly total (>99.5%) block of spontaneous cancer metastasis in vivo. 1 Department of Oncology, University of Alberta, Edmonton, AB T6G 2E1, Canada. 2 Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E9, Canada. 3 Department of Medicine, University of Alberta, Edmonton, AB T6G 2E1, Canada. 4 Department of Laboratory Medicine and Pathology, University of Alberta, Edmonton, AB T6G 2E1, Canada.
[Show full text]