ACD (Human) IP-WB Antibody Pair Gene on Chromosome 11, Which Encodes Tripeptidyl-Peptidase I

Total Page：16

File Type：pdf, Size：1020Kb

ACD (Human) IP-WB Antibody Pair gene on chromosome 11, which encodes tripeptidyl-peptidase I. [provided by RefSeq] Catalog Number: H00065057-PW2 Regulation Status: For research use only (RUO) Product Description: This IP-WB antibody pair set comes with one antibody for immunoprecipitation and another to detect the precipitated protein in western blot. Reactivity: Human Applications: IP-WB (See our web site product page for detailed applications information) Protocols: See our web site at http://www.abnova.com/support/protocols.asp or product page for detailed protocols Supplied Product: Antibody pair set content: 1. Antibody pair for IP: rabbit polyclonal anti-ACD (300 ul) 2. Antibody pair for WB: mouse purified polyclonal anti-ACD (50 ug) Storage Instruction: Store reagents of the antibody pair set at -20°C or lower. Please aliquot to avoid repeated freeze thaw cycle. Reagents should be returned to -20°C storage immediately after use. Entrez GeneID: 65057 Gene Symbol: ACD Gene Alias: PIP1, PTOP, TINT1, TPP1 Gene Summary: This gene encodes a protein that is involved in telomere function. This protein is one of six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with other components, this protein plays a key role in the assembly and stabilization of this complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is also referred to as TPP1, is distinct from the unrelated TPP1 Page 1/1 Powered by TCPDF (www.tcpdf.org).

Copy Link

Recommended publications

Genetics of Familial Non-Medullary Thyroid Carcinoma (FNMTC)
cancers Review Genetics of Familial Non-Medullary Thyroid Carcinoma (FNMTC) Chiara Diquigiovanni * and Elena Bonora Unit of Medical Genetics, Department of Medical and Surgical Sciences, University of Bologna, 40138 Bologna, Italy; [email protected] * Correspondence: [email protected]; Tel.: +39-051-208-8418 Simple Summary: Non-medullary thyroid carcinoma (NMTC) originates from thyroid follicular epithelial cells and is considered familial when occurs in two or more first-degree relatives of the patient, in the absence of predisposing environmental factors. Familial NMTC (FNMTC) cases show a high genetic heterogeneity, thus impairing the identification of pivotal molecular changes. In the past years, linkage-based approaches identified several susceptibility loci and variants associated with NMTC risk, however only few genes have been identified. The advent of next-generation sequencing technologies has improved the discovery of new predisposing genes. In this review we report the most significant genes where variants predispose to FNMTC, with the perspective that the integration of these new molecular findings in the clinical data of patients might allow an early detection and tailored therapy of the disease, optimizing patient management. Abstract: Non-medullary thyroid carcinoma (NMTC) is the most frequent endocrine tumor and originates from the follicular epithelial cells of the thyroid. Familial NMTC (FNMTC) has been defined in pedigrees where two or more first-degree relatives of the patient present the disease in absence of other predisposing environmental factors. Compared to sporadic cases, FNMTCs are often multifocal, recurring more frequently and showing an early age at onset with a worse outcome. FNMTC cases Citation: Diquigiovanni, C.; Bonora, E.
[Show full text]
Structural Genomics Approach to Investigate Deleterious Impact Of
www.nature.com/scientificreports OPEN Structural genomics approach to investigate deleterious impact of nsSNPs in conserved telomere maintenance component 1 Arunabh Choudhury1,5, Taj Mohammad2,5, Nikhil Samarth3, Afzal Hussain4, Md. Tabish Rehman4, Asimul Islam2, Mohamed F. Alajmi4, Shailza Singh3 & Md. Imtaiyaz Hassan2* Conserved telomere maintenance component 1 (CTC1) is an important component of the CST (CTC1-STN1-TEN1) complex, involved in maintaining the stability of telomeric DNA. Several non- synonymous single-nucleotide polymorphisms (nsSNPs) in CTC1 have been reported to cause Coats plus syndrome and Dyskeratosis congenital diseases. Here, we have performed sequence and structure analyses of nsSNPs of CTC1 using state-of-the-art computational methods. The structure- based study focuses on the C-terminal OB-fold region of CTC1. There are 11 pathogenic mutations identifed, and detailed structural analyses were performed. These mutations cause a signifcant disruption of noncovalent interactions, which may be a possible reason for CTC1 instability and consequent diseases. To see the impact of such mutations on the protein conformation, all-atom molecular dynamics (MD) simulations of CTC1-wild-type (WT) and two of the selected mutations, R806C and R806L for 200 ns, were carried out. A signifcant conformational change in the structure of the R806C mutant was observed. This study provides a valuable direction to understand the molecular basis of CTC1 dysfunction in disease progression, including Coats plus syndrome. Unlike prokaryotic chromosomes, eukaryotic chromosomes are linear and are much larger in size. Te ends of the eukaryotic chromosome are composed of a specialized protein-DNA complex called telomeres which maintains the stability of the chromosome ends1.
[Show full text]
Structural and Functional Consequences of a Disease Mutation in the Telomere Protein TPP1
Structural and functional consequences of a disease mutation in the telomere protein TPP1 Kamlesh Bishta,1, Eric M. Smitha,b,1, Valerie M. Tesmera, and Jayakrishnan Nandakumara,b,2 aDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109; and bProgram in Chemical Biology, University of Michigan, Ann Arbor, MI 48109 Edited by Joachim Lingner, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland, and accepted by Editorial Board Member Dinshaw J. Patel September 29, 2016 (received for review April 8, 2016) Telomerase replicates chromosome ends to facilitate continued cell The discovery of the TEL patch of TPP1 prompted the pre- division. Mutations that compromise telomerase function result in diction that this region could be a hotspot for mutations that stem cell failure diseases, such as dyskeratosis congenita (DC). One cause telomerase-deficiency diseases, such as DC. We recently such mutation (K170Δ), residing in the telomerase-recruitment factor reported a case of a severe variant of DC, Hoyeraal–Hreidarsson TPP1, provides an excellent opportunity to structurally, biochemi- syndrome (23), in which the proband was heterozygous for a cally, and genetically dissect the mechanism of such diseases. We deletion of a single amino acid of the TPP1 protein, namely lysine ACD show through site-directed mutagenesis and X-ray crystallography 170 (K170) (24). Our study placed the gene coding for TPP1 DKC1 TERC TERT that this TPP1 disease mutation deforms the conformation of two protein on a list with 10 other genes ( , , , RTEL1 TINF2 CTC1 NOP10 NHP2 WRAP53 PARN critical amino acids of the TEL [TPP1’s glutamate (E) and leucine-rich , , , , , ,and ) that are found mutated in DC and other telomere-related dis- (L)] patch, the surface of TPP1 that binds telomerase.
[Show full text]
REVIEW Telomeres and Telomerase in Adrenocortical Tissue Maintenance
131 REVIEW Telomeres and telomerase in adrenocortical tissue maintenance, carcinogenesis, and aging Tobias Else Division of Metabolism, Endocrinology and Diabetes, MEND/Department of Internal Medicine, University of Michigan Health System, 1860 BSRB, 109 Zina Pitcher Pl, Ann Arbor, Michigan 48109-2200, USA (Correspondence should be addressed to T Else; Email: [email protected]) Abstract Telomere dysfunction and telomere maintenance mechanisms contribute to major steps of carcinogenesis. Dysfunctional telomeres lead to the generation of genomic aberrations, such as amplifications and deletions. Telomere maintenance mechanisms, such as telomerase activity and alternative telomere lengthening, provide the basis of malignant cell expansion independent of telomere shortening-induced apoptosis or senescence, ensuring tumor survival. Recent advances highlight the importance of these mechanisms in adrenocortical carcinogenesis. In this review, we will summarize the main models of telomere physiology and their impact on adrenocortical tissue maintenance, aging, and carcinogenesis. Journal of Molecular Endocrinology (2009) 43, 131–141 Overview cycles (BFBs). An indefinite potential of expansion of malignant cells can be secured by the acquisition Mammalian chromosomes end in a stretch of TTAGGG of telomere length maintenance mechanisms (TMMs), nucleotide repeats known as telomeres. There are two which prevent telomere shortening, either telomerase key challenges inherent to these structures. First, activity (TA)-dependent or TA-independent alternative telomeres need to be protected from being recognized mechanisms of telomere lengthening (ALT). as a form of damaged DNA by the DNA surveillance and Here, we will give insight into the current under- from being processed by the DNA repair machinery. standing of how these problems are solved physio- Second, the semi-conservative DNA replication logically and how they are exploited by malignant cells, machinery does not entirely copy linear chromosomes, specifically those of adrenocortical origin.
[Show full text]
Downregulation of Telomerase Maintenance-Related ACD Expression in Patients Undergoing Immunosuppresive Therapy Following Kidney Transplantation
2224 EXPERIMENTAL AND THERAPEUTIC MEDICINE 10: 2224-2230, 2015 Downregulation of telomerase maintenance-related ACD expression in patients undergoing immunosuppresive therapy following kidney transplantation AGNIESZKA WITKOWSKA1, BARBARA STRZALKA-MROZIK2, ALEKSANDER OWCZAREK3, JOANNA GOLA2, URSZULA MAZUREK2, WLADYSLAW GRZESZCZAK1 and JANUSZ GUMPRECHT1 1Department of Internal Medicine, Diabetology and Nephrology, Medical University of Silesia, 41-800 Zabrze, Silesia; 2Department of Molecular Biology; 3Division of Statistics, Medical University of Silesia, 41-200 Sosnowiec, Silesia, Poland Received August 30, 2014; Accepted July 23, 2015 DOI: 10.3892/etm.2015.2785 Abstract. Chronic administration of immunosuppressants gene transcription, and thus TPP1 protein expression, may has been associated with long-term consequences, including enhance the capacity for cell immortalization, despite normal a higher risk of neoplasm development. The processes regu- levels of other key telomere maintenance factors, in patients lating telomere function exert a major influence on human undergoing immunosuppressive therapy. Furthermore, the cancer biology. The present study aimed to assess the effect of results indicate that TPP1 has potential for use as an early immunosuppressive therapy on the expression of genes asso- clinical marker and/or therapeutic target for cancer in patients ciated with telomere maintenance and protection in patients following organ transplantation. following renal transplantation. A total of 51 patients that had undergone kidney
[Show full text]
Structural and Functional Consequences of a Disease Mutation in the Telomere Protein TPP1
Structural and functional consequences of a disease mutation in the telomere protein TPP1 Kamlesh Bishta,1, Eric M. Smitha,b,1, Valerie M. Tesmera, and Jayakrishnan Nandakumara,b,2 aDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109; and bProgram in Chemical Biology, University of Michigan, Ann Arbor, MI 48109 Edited by Joachim Lingner, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland, and accepted by Editorial Board Member Dinshaw J. Patel September 29, 2016 (received for review April 8, 2016) Telomerase replicates chromosome ends to facilitate continued cell The discovery of the TEL patch of TPP1 prompted the pre- division. Mutations that compromise telomerase function result in diction that this region could be a hotspot for mutations that stem cell failure diseases, such as dyskeratosis congenita (DC). One cause telomerase-deficiency diseases, such as DC. We recently such mutation (K170Δ), residing in the telomerase-recruitment factor reported a case of a severe variant of DC, Hoyeraal–Hreidarsson TPP1, provides an excellent opportunity to structurally, biochemi- syndrome (23), in which the proband was heterozygous for a cally, and genetically dissect the mechanism of such diseases. We deletion of a single amino acid of the TPP1 protein, namely lysine ACD show through site-directed mutagenesis and X-ray crystallography 170 (K170) (24). Our study placed the gene coding for TPP1 DKC1 TERC TERT that this TPP1 disease mutation deforms the conformation of two protein on a list with 10 other genes ( , , , RTEL1 TINF2 CTC1 NOP10 NHP2 WRAP53 PARN critical amino acids of the TEL [TPP1’s glutamate (E) and leucine-rich , , , , , ,and ) that are found mutated in DC and other telomere-related dis- (L)] patch, the surface of TPP1 that binds telomerase.
[Show full text]
POT1 Polyclonal Antibody Catalog # AP72003
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 POT1 Polyclonal Antibody Catalog # AP72003 Specification POT1 Polyclonal Antibody - Product Information Application WB Primary Accession Q9NUX5 Reactivity Human, Monkey Host Rabbit Clonality Polyclonal POT1 Polyclonal Antibody - Additional Information Gene ID 25913 Other Names POT1; Protection of telomeres protein 1; hPot1; POT1-like telomere end-binding protein Dilution WB~~Western Blot: 1/500 - 1/2000. ELISA: 1/10000. Not yet tested in other applications. Format Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. Storage Conditions -20℃ POT1 Polyclonal Antibody - Protein Information Name POT1 Function Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the POT1 Polyclonal Antibody - Background double-stranded telomeric DNA-binding TRF1 complex which is involved in the Component of the telomerase regulation of telomere length by cis- ribonucleoprotein (RNP) complex that is inhibition of telomerase. Also acts as a essential for the replication of chromosome single-stranded telomeric DNA- binding termini. Is a component of the double-stranded protein and thus may act as a downstream telomeric DNA- binding TRF1 complex which is effector of the TRF1 complex and may involved in the regulation of telomere length transduce information about telomere Page 1/2 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 maintenance and/or length to the telomere by cis-inhibition of telomerase. Also acts as a terminus. Component of the shelterin single-stranded telomeric DNA-binding protein complex (telosome) that is involved in the and thus may act as a downstream effector of regulation of telomere length and the TRF1 complex and may transduce protection.
[Show full text]
Shelterin Genes, Germ Line Mutations and Chronic Lymphocytic Leukemia
71 Commentary Shelterin genes, germ line mutations and chronic lymphocytic leukemia Irma Slavutsky Laboratorio de Genética de las Neoplasias Linfoides, Instituto de Medicina Experimental (IMEX), CONICET-Academia Nacional de Medicina, Buenos Aires, Argentina Correspondence to: Irma Slavutsky, MD, PhD. Laboratorio de Genética de Neoplasias Linfoides, Instituto de Medicina Experimental, CONICET- Academia Nacional de Medicina, J.A. Pacheco de Melo 3081, C1425AUM-Buenos Aires, Argentina. Email: [email protected]. Comment on: Speedy HE, Kinnersley B, Chubb D, et al. Germline mutations in shelterin complex genes are associated with familial chronic lymphocytic leukemia. Blood 2016. [Epub ahead of print]. Submitted Jan 06, 2017. Accepted for publication Jan 17, 2017. doi: 10.21037/tcr.2017.02.36 View this article at: http://dx.doi.org/10.21037/tcr.2017.02.36 Telomeres are distinctive DNA-protein structures that studies support a dual role for ACD acting in telomere cap the ends of linear chromosomes; they are essential protection preventing DNA damage response and telomere to maintain chromosomal integrity and genome stability. maintenance, preserving telomere function (4). This Telomeres are composed by tandem repeats of the non- member of the shelterin complex also interacts with ataxia codificante DNA sequence TTAGGG bound by the telangiectasia mutated pathway, thus alterations in ACD may shelterin complex. It contains six core proteins: telomeric stimulate chromosomal instability and large accumulation of repeat binding factor 1 (TERF1), TERF2, protection of mutations leading to cancer development (5). In contrast to the telomeres 1 (POT1), adrenocortical dysplasia homolog other shelterin components, TERF2IP is not a protective (ACD), telomeric repeat-binding factor 2-interacting protein, but prevents telomere recombination and fragility.
[Show full text]
Occurrence, Functionality, and Abundance of the TERT Promoter Mutations
bioRxiv preprint doi: https://doi.org/10.1101/2021.05.03.442397; this version posted June 14, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Occurrence, functionality, and abundance of the TERT promoter mutations Sivaramakrishna Rachakonda1, Jörg D. Hoheisel1, and Rajiv Kumar1,2* 1Division of Functional Genome Analysis, German Cancer Research Center (DKFZ), Heidelberg, Germany 2Department of Molecular Biology of Cancer, Institute of Experimental Medicine of the Czech Academy of Sciences, Videnska, Prague, Czech Republic Keywords: Telomeres, telomerase, TERT promoter mutations, cancers Abbreviations: ACD: Adrenocortical Dysplasia Protein Homolog (unofficial name TPP1); ARF: A-Raf Proto-Oncogene Serine/Threonine-Protein Kinase; ARID2: AT-Rich Interaction Domain 2; ATAC: Assay for Transposase-Accessible Chromatin; BRAF: B-Raf Proto-Oncogene, Serine/Threonine Kinase; CDKN2A: Cyclin-Dependent Kinase Inhibitor 2A; CRAF: C-Raf Proto- Oncogene, Serine/Threonine Kinase; CST: CTC1-STN1-TEN1 complex; CTNNB1: Catenin Beta 1; ENCODE: Encyclopedia of DNA Elements; ELF: E74 Like ETS Transcription Factor; ERK: Extracellular Signal-Regulated Kinase; ETS: E26 Transformation-specific; ETS1: ETS Proto-Oncogene 1, Transcription Factor; ETS2: ETS Proto-Oncogene 2, Transcription Factor; ETV5: ETS Variant Transcription Factor 5; GABPA: GA Binding Protein Transcription Factor Subunit Alpha; GABPB1: GA Binding Protein Transcription Factor Subunit
[Show full text]
A Cell-Specific Regulatory Region of the Human ABO Blood Group Gene
www.nature.com/scientificreports OPEN A cell‑specifc regulatory region of the human ABO blood group gene regulates the neighborhood gene encoding odorant binding protein 2B Rie Sano1*, Yoichiro Takahashi1, Haruki Fukuda1, Megumi Harada1, Akira Hayakawa1, Takafumi Okawa1, Rieko Kubo1, Haruo Takeshita2, Junichi Tsukada3 & Yoshihiko Kominato1 The human ABO blood group system is of great importance in blood transfusion and organ transplantation. ABO transcription is known to be regulated by a constitutive promoter in a CpG island and regions for regulation of cell‑specifc expression such as the downstream + 22.6‑kb site for epithelial cells and a site in intron 1 for erythroid cells. Here we investigated whether the + 22.6‑kb site might play a role in transcriptional regulation of the gene encoding odorant binding protein 2B (OBP2B), which is located on the centromere side 43.4 kb from the + 22.6‑kb site. In the gastric cancer cell line KATOIII, quantitative PCR analysis demonstrated signifcantly reduced amounts of OBP2B and ABO transcripts in mutant cells with biallelic deletions of the site created using the CRISPR/Cas9 system, relative to those in the wild‑type cells, and Western blotting demonstrated a corresponding reduction of OBP2B protein in the mutant cells. Moreover, single‑molecule fuorescence in situ hybridization assays indicated that the amounts of both transcripts were correlated in individual cells. These fndings suggest that OBP2B could be co‑regulated by the + 22.6‑kb site of ABO. Te human ABO blood group system is of great importance in blood transfusion and organ transplantation. Te carbohydrate structures of ABO blood group antigens are produced by the A- and B-transferases encoded by the A and B alleles, respectively1.
[Show full text]
Functional Analysis of ACD Mutations in Dyskeratosis Congenita By
Functional Analysis of ACD Mutations in Dyskeratosis Congenita by Hande Koçak A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Human Genetics) in The University of Michigan 2014 Doctoral Committee: Associate Professor Catherine E. H. Keegan, Chair Professor Sally A. Camper Professor Thomas W. Glover Assistant Professor Jayakrishnan Nandakumar Associate Professor JoAnn M. Sekiguchi © Hande Koçak 2014 DEDIIN To My wonderful parents, Hatice and Basri Yücel Koçak and My wonderful sister, Emine Koçak We made it. ii ACKNOWLEDGEMENTS Foremost, I would like to express my appreciation and thanks to my PhD advisor, Catherine Keegan, for her encouragement, support, and patience. I am sincerely thankful for her research insight and guidance throughout my graduate studies. I am very grateful that Jayakrishnan Nandakumar agreed to become involved in my project and let me spend time in his lab. It is difficult for me to list all that I have learned from him and to express how thankful I am for his help. I cannot find words to express my gratitude to Jayakrishnan Nandakumar, JoAnn Sekiguchi, Thomas Glover and Sally Camper for serving on my thesis committee. They have always been very helpful and supportive. Their advices have kept me focused and goal-oriented during my studies. I have been very lucky to have them in my thesis committee. My special thanks go to JoAnn Sekiguchi for sparing time for me week after week to discuss my data and even just to chat about my concerns. I would like to thank all the former and current members of Keegan Lab.
[Show full text]
ACD Rabbit Pab
Leader in Biomolecular Solutions for Life Science ACD Rabbit pAb Catalog No.: A12177 Basic Information Background Catalog No. This gene encodes a protein that is involved in telomere function. This protein is one of A12177 six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with Observed MW other components, this protein plays a key role in the assembly and stabilization of this 58kDa complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is Calculated MW also referred to as TPP1, is distinct from the unrelated TPP1 gene on chromosome 11, 57kDa which encodes tripeptidyl-peptidase I. Category Primary antibody Applications WB Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 65057 Q96AP0 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-220 of human ACD (NP_001075955.1). Synonyms ACD;PIP1;PTOP;TINT1;TPP1 Contact Product Information 400-999-6126 Source Isotype Purification Rabbit IgG Affinity purification [email protected] www.abclonal.com.cn Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using ACD antibody (A12177) at 1:3000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST.
[Show full text]