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DATASHEET USA: [email protected] FOR IN VITRO RESEARCH USE ONLY Europe: [email protected] NOT FOR USE IN HUMANS OR ANIMALS China: [email protected] MCRS1 Polyclonal Anbody Catalog number: 11362-1-AP Background Size: 45 μg/150 μl MCRS1, also named INO80Q, MSP58 or p78, is a nucleolar protein expressed in the Source: Rabbit very early S phase. It modulates the transcripon repressor acvity of DAXX by Isotype: IgG recruing it to the nucleolus. MCRS1 is also present on polyribosomes of Synonyms: synaptoneurosome as a novel RNA-binding protein to acvate the rRNA MCRS1; 58 kDa microspherule transcripon. The forkhead-associated domain of MCRS1 is involved in associaon protein, ICP22BP, INO80 with centrosomal protein Nde1, comprising a component of the centrosome and complex subunit J, INO80Q, taking an essenal role in viability. Its isoform MCRS2 might be a linker between MCRS1, MCRS2, microspherule telomere maintenance and cell-cycle regulaon by interacng with LPTS/PinX1, a protein 1, MSP58, P78 telomerase-inhibitory protein. MCRS1 is detected by Western blot as a highly modified protein at 78 kDa and minor bands at about 62 and 55 kDa. Applications Tested applicaons: ELISA, WB Cited applicaons: WB Species specificity: Human,Mouse,Rat; other species not tested. Cited species: Human, mouse HeLa cells were subjected to SDS Caculated MCRS1 MW: 51 kDa PAGE followed by western blot with 11362-1-AP(MCRS1 anbody) at Observed MCRS1 MW: 55 kDa diluon of 1:500 Posive WB detected in HeLa cells, human brain ssue, human liver ssue, human spleen ssue, Jurkat cells, mouse spleen ssue, mouse uterus ssue, rat spleen ssue Recommended diluon: WB: 1:500-1:5000 Applicaon key: WB = Western blong, IHC = Immunohistochemistry, IF = Immunofluorescence, IP = Immunoprecipitaon Immunogen information Immunogen: Ag1904 GenBank accession number: BC011794 Gene ID (NCBI): 10445 Full name: Microspherule protein 1 Product information Purificaon method: Angen affinity purificaon Storage: PBS with 0.1% sodium azide and 50% glycerol pH 7.3. Store at -20oC..

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Pinx1: Structure, Regulation and Its Functions in Cancer
www.impactjournals.com/oncotarget/ Oncotarget, Vol. 7, No. 40 Review PinX1: structure, regulation and its functions in cancer Hai-Long Li1,2,*, Jun Song3,4,*, Hong-Mei Yong5,*, Ping-Fu Hou1,3, Yan-Su Chen1,3, Wen-Bo Song1, Jin Bai1 and Jun-Nian Zheng1,3 1 Jiangsu Key Laboratory of Biological Cancer Therapy, Xuzhou Medical College, Xuzhou, Jiangsu, China 2 Department of Urology, The Affiliated Hospital of Xuzhou Medical College, Xuzhou, Jiangsu, China 3 Jiangsu Center for the Collaboration and Innovation of Cancer Biotherapy, Cancer Institute, Xuzhou Medical College, Xuzhou, Jiangsu, China 4 Department of General Surgery, The Affiliated Hospital of Xuzhou Medical College, Xuzhou, Jiangsu, China 5 Department of Medical Oncology, Huai’an Hospital to Xuzhou Medical College, Huai’an, Jiangsu, China * These authors have contributed equally to this study Correspondence to: Jun-Nian Zheng, email: [email protected] Correspondence to: Jin Bai, email: [email protected] Keywords: PinX1; cancer; structure; regulation; function Received: March 14, 2016 Accepted: August 09, 2016 Published: August 19, 2016 ABSTRACT PIN2/TRF1-interacting telomerase inhibitor 1 (PinX1) is a novel cloned gene located at human chromosome 8p23, playing a vital role in maintaining telomeres length and chromosome stability. It has been demonstrated to be involved in tumor genesis and progression in most malignancies. However, some researches showed opposing molecular status of PinX1 gene and its expression patterns in several other types of tumors. The pathogenic mechanism of PinX1 expression in human malignancy is not yet clear. Moreover, emerging evidence suggest that PinX1 (especially its TID domain) might be a potential new target cancer treatment.
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Expression of MCRS1 and MCRS2 and Their Correlation with Serum Carcinoembryonic Antigen in Colorectal Cancer
EXPERIMENTAL AND THERAPEUTIC MEDICINE 12: 589-596, 2016 Expression of MCRS1 and MCRS2 and their correlation with serum carcinoembryonic antigen in colorectal cancer CHENGUANG LI1,2, MINGXIAO CHEN1, PINGWEI ZHAO1, DESALEGN ADMASSU AYANA3, LEI WANG1 and YANFANG JIANG2 1Department of Colorectal and Anal Surgery, The First Hospital, Jilin University, Changchun, Jilin 130032; 2Key Laboratory of Zoonosis Research, Ministry of Education, The First Hospital, Jilin University, Changchun, Jilin 130032, P.R. China; 3Department of Medical Laboratory Sciences, Haramaya University, Dire Dawa 3000, Ethiopia Received June 30, 2015; Accepted March 3, 2016 DOI: 10.3892/etm.2016.3424 Abstract. Cancer-associated genes serve a crucial role in patients with CRC. The results suggest that increased MCRS1 carcinogenesis. The present study aimed to investigate the and decreased MCRS2 expression appeared to be involved mRNA expression levels of microspherule protein 1 (MCRS1) in the pathogenesis of CRC. The present study provides and MCRS2 in colorectal cancer (CRC) and their associa- evidence suggesting that MCRS1 and MCRS2 may identify tion with clinical variables. The mRNA expression levels of CRC patients at a risk of disease relapse, and thus, may be MCRS1 and MCRS2 were assessed by semi-quantitative potential tools for monitoring disease activity and act as novel reverse transcription polymerase chain reaction in the tumor diagnostic markers in the treatment of CRC. and corresponding non-tumor tissues of 54 newly-diagnosed CRC patients, as well as in the normal colonic mucosa tissue of Introduction 19 age/gender‑matched healthy controls. Immunofluorescence was also employed to identify the expression of MCRS1 in Colorectal cancer (CRC) is one of the most prevalent malig- CRC tissues, while the concentration of serum carcinoem- nant tumors, with high incidence rate and mortality.
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DNA Binding Features of Human POT1 a NONAMER 5Ј-TAGGGTTAG-3Ј MINIMAL BINDING SITE, SEQUENCE SPECIFICITY, and INTERNAL BINDING to MULTIMERIC SITES*
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Association Between the PINX1 and NAT2 Polymorphisms and Serum Lipid Levels
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Supplemental Table 1 Telomere Pathway Genes Evaluated in the Current Study
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MCRS1 Associates with Cytoplasmic Dynein and Mediates
www.nature.com/scientificreports OPEN MCRS1 associates with cytoplasmic dynein and mediates pericentrosomal material Received: 14 March 2016 Accepted: 13 May 2016 recruitment Published: 06 June 2016 Si-Hyung Lee1, Mi-Sun Lee2, Tae-Ik Choi2, Hyowon Hong1, Jun-Young Seo3, Cheol-Hee Kim2 & Joon Kim1 MCRS1 is involved in multiple cellular activities, including mitotic spindle assembly, mTOR signaling and tumorigenesis. Although MCRS1 has been reported to bind to the dynein regulator NDE1, a functional interaction between MCRS1 and cytoplasmic dynein remains unaddressed. Here, we demonstrate that MCRS1 is required for dynein-dependent cargo transport to the centrosome and also plays a role in primary cilium formation. MCRS1 localized to centriolar satellites. Knockdown of MCRS1 resulted in a dispersion of centriolar satellites whose establishment depends on cytoplasmic dynein. By contrast, NDE1 was not necessary for the proper distribution of centriolar satellites, indicating a functional distinction between MCRS1 and NDE1. Unlike NDE1, MCRS1 played a positive role for the initiation of ciliogenesis, possibly through its interaction with TTBK2. Zebrafish with homozygous mcrs1 mutants exhibited a reduction in the size of the brain and the eye due to excessive apoptosis. In addition, mcrs1 mutants failed to develop distinct layers in the retina, and showed a defect in melatonin-induced aggregation of melanosomes in melanophores. These phenotypes are reminiscent of zebrafish dynein mutants. Reduced ciliogenesis was also apparent in the olfactory placode ofmcrs1 mutants. Collectively, our findings identify MCRS1 as a dynein-interacting protein critical for centriolar satellite formation and ciliogenesis. Microspherule protein 1 (MCRS1) and its isoform 58-kDa microspherule protein (MSP58) are localized to electron dense bodies within the nucleoli, designated as microspherules1.
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Aberrant Telomere Structure Is Characteristic of Resistant Chronic Lymphocytic Leukaemia Cells
Letters to the Editor 246 7 Life Sciences Division, Department of Statistics, University of 3 Michaud J, Simpson KM, Escher R, Buchet-Poyau K, Beissbarth T, California, Lawrence Berkeley National Laboratory, Carmichael C et al. Integrative analysis of RUNX1 downstream Berkeley, CA, USA and pathways and target genes. BMC Genomics 2008; 31: 363. 8Department of Pediatric Hemato-oncology, Radboud 4 Mikhail FM, Sinha KK, Saunthararajah Y, Nucifora G. Normal and University Nijmegen Medical Center, Nijmegen, transforming functions of RUNX1: a perspective. J Cell Physiol The Netherlands 2006; 207: 582–593. E-mails: [email protected] or 5 Renneville A, Roumier C, Biggio V, Nibourel O, Boissel N, [email protected] Fenaux P et al. Cooperating gene mutations in acute myeloid 9These authors contributed equally to this work. leukemia: a review of the literature. Leukemia 2008; 22: 915–931. 6 Ripperger T, Steinemann D, Go¨hring G, Finke J, Niemeyer CM, Strahm B et al. A novel pedigree with heterozygous germline RUNX1 mutation causing familial MDS-related AML: can these families serve as a multistep model for leukemic transformation? References Leukemia 2009; 23: 1364–1366. 7 Michaud J, Wu F, Osato M, Cottles GM, Yanagida M, Asou N et al. 1 Owen CJ, Toze CL, Koochin A, Forrest DL, Smith CA, Stevens JM In vitro analyses of known and novel RUNX1/AML1 mutations in et al. Five new pedigrees with inherited RUNX1 mutations causing dominant familial platelet disorder with predisposition to acute familial platelet disorder with propensity to myeloid malignancy. myelogenous leukemia: implications for mechanisms of pathogen- Blood 2008; 112: 4639–4645.
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And Attenuates the Pinx1 Inhibition on Telomerase Activity
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