ST14 Rabbit Pab

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Leader in Biomolecular Solutions for Life Science ST14 Rabbit pAb Catalog No.: A6135 Basic Information Background Catalog No. The protein encoded by this gene is an epithelial-derived, integral membrane serine A6135 protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been Observed MW shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase 95kDa plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of Calculated MW this protease has been associated with breast, colon, prostate, and ovarian tumors, 94kDa which implicates its role in cancer invasion, and metastasis. Category Primary antibody Applications WB Cross-Reactivity Human, Mouse Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 6768 Q9Y5Y6 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 566-855 of human ST14 (NP_068813.1). Synonyms ST14;ARCI11;HAI;MT-SP1;MTSP1;PRSS14;SNC19;TADG15;TMPRSS14 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 ST14 antibody (A6135) at 1:1000 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. Detection: ECL Basic Kit (RM00020). Exposure time: 60s. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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The Genetical Society of Great Britain
Heredity 59 (1987) 151—160 The Genetical Society of Great Britain THEGENETICAL SOCIETY (Abstracts of papers presented at the TVVO HUNDRED AND FIFTH MEETING of the Society held on Friday, 14th and Saturday, 15th November 1986 at UNIVERSITY COLLEGE, LONDON) 1. Selection of somatic cell D. J. Porteous, P. A. Boyd, N. D. Hastie and hybrids with specific chromosome V. van Heyningen content for mapping the WAGR MAC Clinical and Population Cytogenetics Unit, Western General Hospital, Crewe Road, syndrome Edinburgh EH4 2XU. J. M. Fletcher, H. Morrison, J. A. Fantes, Clonedprobes for a number of available chromo- A. Seawright, S. Christie, D. J. Porteous, some ii assigned genes were used to define the N. D. Hastie and V. van Heyningen extent of deletions associated with the Wilms' MAC Clinical and Population Cytogenetics Unit, tumour, aniridia, genitourinary abnormalities and Western General Hospital, Crewe Road, mental retardation (WAGR) syndrome. Establish- Edinburgh EH4 2XU. ing reliable dosage studies for a number of different probes has proved difficult. We have therefore WAGR(Wilms tumour, aniridia, genitourinary abnormalities and mental retardation) syndrome concentrated on segregating the deleted chromo- is frequently associated with deletions on the short some 11 from a number of patients in somatic cell arm of chromosome 11. The deletions vary in size hybrids and analysing DNA from these to produce but always include part of band lipl3. To home a consistent map of chromosome lip. At the same in on the Wilms tumour and aniridia loci the end time we have determined the deletion breakpoints points of the different deletion breakpoints need at a molecular level and shown that the results are to be defined at the DNA level.
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Screening and Identification of Key Biomarkers in Clear Cell Renal Cell Carcinoma Based on Bioinformatics Analysis
bioRxiv preprint doi: https://doi.org/10.1101/2020.12.21.423889; this version posted December 23, 2020. 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. Screening and identification of key biomarkers in clear cell renal cell carcinoma based on bioinformatics analysis Basavaraj Vastrad1, Chanabasayya Vastrad*2 , Iranna Kotturshetti 1. Department of Biochemistry, Basaveshwar College of Pharmacy, Gadag, Karnataka 582103, India. 2. Biostatistics and Bioinformatics, Chanabasava Nilaya, Bharthinagar, Dharwad 580001, Karanataka, India. 3. Department of Ayurveda, Rajiv Gandhi Education Society`s Ayurvedic Medical College, Ron, Karnataka 562209, India. * Chanabasayya Vastrad [email protected] Ph: +919480073398 Chanabasava Nilaya, Bharthinagar, Dharwad 580001 , Karanataka, India bioRxiv preprint doi: https://doi.org/10.1101/2020.12.21.423889; this version posted December 23, 2020. 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. Abstract Clear cell renal cell carcinoma (ccRCC) is one of the most common types of malignancy of the urinary system. The pathogenesis and effective diagnosis of ccRCC have become popular topics for research in the previous decade. In the current study, an integrated bioinformatics analysis was performed to identify core genes associated in ccRCC. An expression dataset (GSE105261) was downloaded from the Gene Expression Omnibus database, and included 26 ccRCC and 9 normal kideny samples. Assessment of the microarray dataset led to the recognition of differentially expressed genes (DEGs), which was subsequently used for pathway and gene ontology (GO) enrichment analysis.
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SPINT1) by Transcription Published: Xx Xx Xxxx Factor CDX2 E
www.nature.com/scientificreports OPEN Intestinal regulation of suppression of tumorigenicity 14 (ST14) and serine peptidase inhibitor, Kunitz Received: 5 April 2018 Accepted: 23 July 2018 type -1 (SPINT1) by transcription Published: xx xx xxxx factor CDX2 E. Thomas Danielsen 1,2, Anders Krüger Olsen2, Mehmet Coskun3, Annika W. Nonboe2, Sylvester Larsen 1,4, Katja Dahlgaard1, Eric Paul Bennett5, Cathy Mitchelmore1, Lotte Katrine Vogel2 & Jesper Thorvald Troelsen 1 The type II membrane-anchored serine protease, matriptase, encoded by suppression of tumorgenicity-14 (ST14) regulates the integrity of the intestinal epithelial barrier in concert with its inhibitor, HAI-1 encoded by serine peptidase inhibitor, Kunitz type -1 (SPINT1). The balance of the protease/inhibitor gene expression ratio is vital in preventing the oncogenic potential of matriptase. The intestinal cell lineage is regulated by a transcriptional regulatory network where the tumor suppressor, Caudal homeobox 2 (CDX2) is considered to be an intestinal master transcription factor. In this study, we show that CDX2 has a dual function in regulating both ST14 and SPINT1, gene expression in intestinal cells. We fnd that CDX2 is not required for the basal ST14 and SPINT1 gene expression; however changes in CDX2 expression afects the ST14/SPINT1 mRNA ratio. Exploring CDX2 ChIP-seq data from intestinal cell lines, we identifed genomic CDX2-enriched enhancer elements for both ST14 and SPINT1, which regulate their corresponding gene promoter activity. We show that CDX2 displays both repressive and enhancing regulatory abilities in a cell specifc manner. Together, these data reveal new insight into transcriptional mechanisms controlling the intestinal matriptase/inhibitor balance.
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SARS-Cov-2 Entry Protein TMPRSS2 and Its Homologue, TMPRSS4
bioRxiv preprint doi: https://doi.org/10.1101/2021.04.26.441280; this version posted April 26, 2021. 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-NC-ND 4.0 International license. 1 SARS-CoV-2 Entry Protein TMPRSS2 and Its 2 Homologue, TMPRSS4 Adopts Structural Fold Similar 3 to Blood Coagulation and Complement Pathway 4 Related Proteins ∗,a ∗∗,b b 5 Vijaykumar Yogesh Muley , Amit Singh , Karl Gruber , Alfredo ∗,a 6 Varela-Echavarría a 7 Instituto de Neurobiología, Universidad Nacional Autónoma de México, Querétaro, México b 8 Institute of Molecular Biosciences, University of Graz, Graz, Austria 9 Abstract The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) utilizes TMPRSS2 receptor to enter target human cells and subsequently causes coron- avirus disease 19 (COVID-19). TMPRSS2 belongs to the type II serine proteases of subfamily TMPRSS, which is characterized by the presence of the serine- protease domain. TMPRSS4 is another TMPRSS member, which has a domain architecture similar to TMPRSS2. TMPRSS2 and TMPRSS4 have been shown to be involved in SARS-CoV-2 infection. However, their normal physiological roles have not been explored in detail. In this study, we analyzed the amino acid sequences and predicted 3D structures of TMPRSS2 and TMPRSS4 to under- stand their functional aspects at the protein domain level. Our results suggest that these proteins are likely to have common functions based on their conserved domain organization.
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ST14 (NM 021978) Human 3' UTR Clone – SC207486 | 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 SC207486 ST14 (NM_021978) Human 3' UTR Clone Product data: Product Type: 3' UTR Clones Product Name: ST14 (NM_021978) Human 3' UTR Clone Vector: pMirTarget (PS100062) Symbol: ST14 Synonyms: ARCI11; CAP3; HAI; MT-SP1; MTSP1; PRSS14; SNC19; TADG15; TMPRSS14 ACCN: NM_021978 Insert Size: 569 bp Insert Sequence: >SC207486 3’UTR clone of NM_021978 The sequence shown below is from the reference sequence of NM_021978. The complete sequence of this clone may contain minor differences, such as SNPs. Blue=Stop Codon Red=Cloning site GGCAAGTTGGACGCCCGCAAGATCCGCGAGATTCTCATTAAGGCCAAGAAGGGCGGAAAGATCGCCGTG TAACAATTGGCAGAGCTCAGAATTCAAGCGATCGCC GACTGGATCAAAGAGAACACTGGGGTATAGGGGCCGGGGCCACCCAAATGTGTACACCTGCGGGGCCAC CCATCGTCCACCCCAGTGTGCACGCCTGCAGGCTGGAGACTGGACCGCTGACTGCACCAGCGCCCCCAG AACATACACTGTGAACTCAATCTCCAGGGCTCCAAATCTGCCTAGAAAACCTCTCGCTTCCTCAGCCTC CAAAGTGGAGCTGGGAGGTAGAAGGGGAGGACACTGGTGGTTCTACTGACCCAACTGGGGGCAAAGGTT TGAAGACACAGCCTCCCCCGCCAGCCCCAAGCTGGGCCGAGGCGCGTTTGTGCATATCTGCCTCCCCTG TCTCTAAGGAGCAGCGGGAACGGAGCTTCGGGGCCTCCTCAGTGAAGGTGGTGGGGCTGCCGGATCTGG GCTGTGGGGCCCTTGGGCCACGCTCTTGAGGAAGCCCAGGCTCGGAGGACCCTGGAAAACAGACGGGTC TGAGACTGAAATTGTTTTACCAGCTCCCAGGGTGGACTTCAGTGTGTGTATTTGTGTAAATGAGTAAAA CATTTTATTTCTTTTTA ACGCGTAAGCGGCCGCGGCATCTAGATTCGAAGAAAATGACCGACCAAGCGACGCCCAACCTGCCATCA CGAGATTTCGATTCCACCGCCGCCTTCTATGAAAGG Restriction Sites: SgfI-MluI OTI Disclaimer:
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Downloaded on 14Th December 2017 from SKCM 200E, 200 Kv, 4.5 Ma) 2 Days Before the Transplantation
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Hepatocyte Growth Factor Activator Inhibitor Type 1 Regulates Epithelial to Mesenchymal Transition Through Membrane-Bound Serine Proteinases
Published OnlineFirst February 17, 2009; DOI: 10.1158/0008-5472.CAN-08-3728 Research Article Hepatocyte Growth Factor Activator Inhibitor Type 1 Regulates Epithelial to Mesenchymal Transition through Membrane-Bound Serine Proteinases Haixia Cheng, Tsuyoshi Fukushima, Nobuyasu Takahashi, Hiroyuki Tanaka, and Hiroaki Kataoka Section of Oncopathology and Regenerative Biology, Department of Pathology, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan Abstract skin (1). It is also strongly expressed by placental cytotrophoblasts Hepatocyte growth factor activator inhibitor-1 (HAI-1), (2). HAI-1/SPINT1 is composed of an extracellular domain con- encoded by the serine protease inhibitor Kunitz type 1 (SPINT1) taining an NH2-terminal Kunitz domain (KD1), a low-density gene, is a membrane-associated proteinase inhibitor that lipoprotein receptor (LDLR)–like domain and a COOH-terminal potently inhibits a variety of serine proteinases, including Kunitz domain (KD2), followed by a transmembrane region and a those that are membrane bound. Although HAI-1/SPINT1 is short cytoplasmic domain (3, 4). To date, only a few examples of membrane-associated serine proteinase inhibitors have been widely expressed by epithelial cells and cancer cells, its in vivo functional role is still unclear, particularly in cancer. Here, we reported (4, 5), and HAI-1/SPINT1 seems to have roles show that stable knockdown of HAI-1/SPINT1 in the human that are both unique and important (6). Previous studies showed pancreatic cancer cell line SUIT-2 induces an elongated that HAI-1/SPINT1 potently inhibits the action of a variety of trypsin-like serine proteinases that may be involved in carcino- spindle-like morphology associated with accelerated invasion, thereby mimicking an epithelial to mesenchymal transition genesis, invasion, and metastasis.
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Hepatocyte Growth Factor Activator Inhibitor Type 1 (Hai-1/Spint1) Is a Suppressor of Intestinal Tumorigenesis
Author Manuscript Published OnlineFirst on February 27, 2013; DOI: 10.1158/0008-5472.CAN-12-3337 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Hepatocyte growth factor activator inhibitor type 1 (Hai-1/Spint1) is a suppressor of intestinal tumorigenesis Shinri Hoshiko,*,# Makiko Kawaguchi,* Tsuyoshi Fukushima,* Yukihiro Haruyama,* Kenji Yorita,* Hiroyuki Tanaka,* Motoharu Seiki,‡ Haruhiko Inatsu,# Kazuo Kitamura# and Hiroaki Kataoka* *Section of Oncopathology and Regenerative Biology, Department of Pathology and #Section of Circulatory and Body Fluid Regulation, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan; ‡Division of Cancer Cell Research, Institute of Medical Science, The University of Tokyo, Tokyo, Japan. S.H. and M.K. contributed equally to this study Running title: HAI-1 suppresses intestinal tumorigenesis Key words: HAI-1, carcinogenesis, colon cancer, hepatocyte growth factor, epithelial integrity Financial support: This work was supported by Grant-in-Aid for Scientific Research no. 24390099 (H.K.) and no. 23790250 (M.K.) from the Ministry of Education, Science, Sports and Culture, Japan. Corresponding author: Hiroaki Kataoka, Section of Oncopathology and Regenerative Biology, Department of Pathology, Faculty of Medicine, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan. Phone, +81-985-852809; Fax, +81-985-856003; E-mail, [email protected] 1 Downloaded from cancerres.aacrjournals.org on October 2, 2021. © 2013 American Association for Cancer Research. Author Manuscript Published OnlineFirst on February 27, 2013; DOI: 10.1158/0008-5472.CAN-12-3337 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited.
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Published OnlineFirst August 17, 2010; DOI: 10.1158/1055-9965.EPI-10-0418 Published OnlineFirst on August 17, 2010 as 10.1158/1055-9965.EPI-10-0418 Cancer Research Article Epidemiology, Biomarkers & Prevention ST14 Gene Variant and Decreased Matriptase Protein Expression Predict Poor Breast Cancer Survival Jaana M. Kauppinen1, Veli-Matti Kosma1, Ylermi Soini1, Reijo Sironen1, Minna Nissinen1, Timo K. Nykopp1, Vesa Kärjä1, Matti Eskelinen2, Vesa Kataja3, and Arto Mannermaa1 Abstract Background: Matriptase plays a role in carcinogenesis, but the role of its genetic variation or that of the hepatocyte growth factor activator inhibitor-1 (HAI-1) has not been evaluated. This study aimed to examine the genetic variation of matriptase (ST14 gene) and HAI-1 (SPINT1 gene) in breast cancer risk and prognosis, to assess matriptase and HAI-1 gene and protein expression in breast tumors, and to identify their clinico- pathologic correlations and prognostic significance. Methods: Five single nucleotide polymorphisms in ST14 and three in SPINT1 were genotyped in 470 in- vasive breast cancer cases and 446 healthy controls. Gene expression analysis was done for 40 breast cancer samples. Protein expression was assessed by immunohistochemical analyses in 377 invasive breast tumors. The statistical significance of the associations among genotypes, clinicopathologic variables, and prognosis was assessed. Results: The ST14 single nucleotide polymorphism rs704624 independently predicted breast cancer surviv- al, a poor outcome associated with the minor allele (P = 0.001; risk ratio, 2.221; 95% confidence interval, 1.382- 3.568). Moreover, ST14 gene expression levels were lower among the minor allele carriers (P = 0.009), and negative/low matriptase protein expression was independently predictive of poorer survival (P = 0.046; risk ratio, 1.554; 95% confidence interval, 1.008-2.396).
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Immune Deficiency in Jacobsen Syndrome: Molecular And
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