DOCSLIB.ORG

Haemostasis Antibodies from Cedarlane

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Haemostasis Antibodies from Cedarlane HAEMOSTASIS ANTIBODIES FROM CEDARLANE Haemostasis Antibodies www.cedarlanelabs.com Haemostasis Antibodies The study of haemostasis and thrombosis has become one of the most rapidly growing fields in medical research. An unprecedented amount of research is currently focused on the study of the regulatory mechanisms involved in blood clot formation, subsequent lysis, and potential pharmacological intervention of these processes. Cedarlane offers a complete line of antibodies to haemostasis related antigens. The high quality and purity of these antibodies make them valuable tools for applications including ELISA, immunohistochemistry, immunoblotting (Western blot) and immunoprecipitation techniques (including immunodiffusion and rocket immunoelectrophoresis). Haemostasis Antibodies Haemostasis NEW! Cedarlane offers an expanding range of new monoclonal antibodies to various haemostasis related antigens, providing customers a more comprehensive array of tools for the study of haemostasis and thrombosis. These antibodies have been tested for suitability for use in Western Blotting and ELISA. Featured Antibodies Specificity Format Clone Isotype Species Application Size Cat # Price $ Reactivity Factor VII/VIIA Purified AA-3 mouse IgG1 Human E, WB 200 μg CL2763AP 259 Factor VII/VIIA Biotin AA-3 mouse IgG1 Human E, WB 100 μg CL2763B 199 Factor VII/VIIa Purified AD-1 mouse IgG1 Human E, WB 200 μg CL2764AP 259 Factor VII/VIIa Biotin AD-1 mouse IgG1 Human E, WB 100 μg CL2764B 199 Factor VII/VIIa (Calcium Dependent) Purified CaFVII-22 mouse IgG1 Human E, WB 200 μg CL2762AP 259 Factor VII/VIIa (Calcium Dependent) Biotin CaFVII-22 mouse IgG1 Human E, WB 100 μg CL2762B 199 Factor IX/IXa (Calcium Dependent) Purified CaFIX-1 mouse IgG1 Human E, WB 200 μg CL2765AP 259 Factor IX/IXa (Calcium Dependent) Biotin CaFIX-1 mouse IgG1 Human E, WB 100 μg CL2765B 199 Factor X/Xa (Calcium Dependent) Purified CaFX-50 mouse IgG1 Human E, WB 200 μg CL2768AP 259 Factor X/Xa (Calcium Dependent) Biotin CaFX-50 mouse IgG1 Human E, WB 100 μg CL2768B 199 Platelet Factor 4 Purified RTO mouse IgG2b Human E, WB 200 μg CL2766AP 259 Platelet Factor 4 Biotin RTO mouse IgG2b Human E, WB 100 μg CL2766B 199 Platelet Factor 4 (requires heparin for binding) Purified KKO mouse IgG2b Human E, WB 200 μg CL2767AP 259 Platelet Factor 4 (requires heparin for binding) Biotin KKO mouse IgG2b Human E, WB 100 μg CL2767B 199 Protein C/APC (Calcium Dependent) Purified CaC-11 mouse IgG1 Human E, WB 200 μg CL2769AP 259 Proteinase Inhibitor 8 Purified anti-PI8K mouse IgG1 Human E, WB 200 μg CL2770AP 259 Prothrombin (Calcium Dependent) Purified CaPro-20 mouse IgG1 Human E, WB 200 μg CL2761AP 259 Prothrombin (Calcium Dependent) Biotin CaPro-20 mouse IgG1 Human E, WB 100 μg CL2761B 199 Legend for Applications: AC=Affinity Chromatography AGG=Agglutination C=Cryostat Sections CT=Cytotoxicity Assay D=Depletion E=ELISA EC=ELISA (Capture) ED=ELISA (Detection) F=Flow Cytometry FN=Functional Assay IC=Immunocytochemistry ID=Immunodiffusion IF=Immunofluorescence IP=Immunoprecipitation IV=In vivo Assay N=Neutralization P=Paraffin-Embedded Sections R=RIA WB=Western Blotting Cedarlane’s Buffer Pack NEW! Cat # CL20300 Price (USD): $ 239.00 Cedarlane’s Buffer Pack for Haemostasis Paired Antibodies consists of assay plates, general purpose buffers and materials for the preparation and performance of ELISA assays. This Buffer Pack provides sufficient reagents for 5 x 96 well assays. The components of the Buffer Pack can be used in the development of in-house immunoassays and are especially suited for use with a number of Cedarlane’s paired antibody sets, including the following: CL20067K CL20067K-RB CL20111K CL20225K CL20030K CL20403K CL20245K CL20250K CL20055K CL20057K CL20096K CL20106K CL20295K CL20201K CL20220K CL20086K CL20003K CL20002K CL20027K CL20090K CL20200K CL20116K CL20017K CL20048K CL20049K CL20087K 2 HAEMOSTASIS ANTIBODIES FROM CEDARLANE Working concentrations for ELISA and Immunoblotting applications General recommendations only and may not apply to all products listed. For more information, please contact [email protected] or your local distributor. Haemostasis Antibodies Haemostasis Format Immunoblotting (ECL detection) ELISA (capture) ELISA (detecting) Purified (Whole IgG) 5–25 μg/ml 20–50 μg/ml NA Affinity Purified 0.5–5 μg/ml 10 μg/ml NA HRPO (Peroxidase-labelled IgG) 5 μg/ml NA 10 μg/ml HRPO (Aff. Pur. Peroxidase-labelled IgG) 1 μg/ml NA 2 μg/ml Haemostasis Antibodies Specificity Format Clone Isotype Species Application Size Cat # Price $ Reactivity α1-Antitrypsin Purified sheep IgG Human IP 10 mg CL20000A 96 α1-Antitrypsin Affinity Purified sheep IgG Human E 0.5 mg CL20000AP 184 α1-Antitrypsin HRPO (Affinity Pur) sheep IgG Human E 0.1 mg CL20000APHP 162 α1-Antitrypsin Purified goat IgG Human IP 10 mg CL20001A 108 α1-Antitrypsin Affinity Purified goat IgG Human E 0.5 mg CL20001AP 184 α2-Antiplasmin Purified goat IgG Human IP, D 5 mg CL20005A 136 α2-Antiplasmin Affinity Purified goat IgG Human E 0.5 mg CL20005AP 262 α2-Antiplasmin HRPO goat IgG Human E 0.2 mg CL20005HP 209 α2-Antiplasmin Purified sheep IgG Human E 10 mg CL20006A 146 α2-Macroglobulin Purified goat IgG Human IP 10 mg CL20010A 96 α2-Macroglobulin Affinity Purified goat IgG Human E, WB 0.5 mg CL20010AP 184 α2-Macroglobulin HRPO (Affinity Pur) goat IgG Human E, WB 0.1 mg CL20010APHP 162 Antithrombin III Inhibitor and Control Antibodies Human N 10 det CL20007N 116 Antithrombin III Purified sheep IgG Human N, D, IP 10 mg CL20015A 80 Antithrombin III Affinity Purified sheep IgG Human E, WB, IP 0.5 mg CL20015AP 209 Antithrombin III HRPO (Affinity Pur) sheep IgG Human E, WB 0.1 mg CL20015APHP 186 Antithrombin III Biotin sheep IgG Human E, WB 0.1 mg CL20015B 186 Antithrombin III FITC sheep IgG Human IF 0.1 mg CL20015F 186 Antithrombin III Purified goat IgG Human IP, N, D 10 mg CL20016A 96 Antithrombin III Affinity Purified goat IgG Human E, IP 0.5 mg CL20016AP 236 Antithrombin III Purified sheep IgG Rabbit E, IP 10 mg CL20018A-RB 117 Antithrombin III Affinity Purified sheep IgG Rabbit E, IP 0.5 mg CL20018AP-RB 249 Antithrombin III HRPO sheep IgG Rabbit E 0.2 mg CL20018HP-RB 209 Complement Component C1 Esterase Purified goat IgG Human IP 5 mg CL20023A 162 Inhibitor (C1 Inactivator) Complement Component C1 Esterase Affinity Purified goat IgG Human E, IP 0.5 mg CL20023AP 292 Inhibitor (C1 Inactivator) Complement Component C1 Esterase HRPO goat IgG Human E 0.2 mg CL20023HP 209 Inhibitor (C1 Inactivator) Factor H Purified OX-24 mouse IgG1 Human E 250 μg CL7672AP 200 Factor H Biotin OX-24 mouse IgG1 Human E 100 μg CL7672B 115 Factor H FITC OX-24 mouse IgG1 Human E 100 μg CL7672F 126 Legend for Applications: AC=Affinity Chromatography AGG=Agglutination C=Cryostat Sections CT=Cytotoxicity Assay D=Depletion E=ELISA EC=ELISA (Capture) ED=ELISA (Detection) F=Flow Cytometry FN=Functional Assay IC=Immunocytochemistry ID=Immunodiffusion IF=Immunofluorescence IP=Immunoprecipitation IV=In vivo Assay N=Neutralization P=Paraffin-Embedded Sections R=RIA WB=Western Blotting HAEMOSTASIS ANTIBODIES FROM CEDARLANE 3 Haemostasis Antibodies (continued) Specificity Format Clone Isotype Species Application Size Cat # Price $ Reactivity Factor IX Purified sheep IgG Human E 10 mg CL20039A 136 Factor IX Affinity Purified sheep IgG Human EC 0.5 mg CL20039AP 249 Factor IX HRPO (Affinity Pur) sheep IgG Human E 0.1 mg CL20039APHP 182 Factor IX Purified goat IgG Human IP, D, WB 10 mg CL20040A 122 Factor IX Affinity Purified goat IgG Human E 0.5 mg CL20040AP 249 Factor IX HRPO (Affinity Pur) goat IgG Human E, WB 0.1 mg CL20040APHP 182 Haemostasis Antibodies Haemostasis Factor IX Biotin goat IgG Human E, WB 0.1 mg CL20040B 182 Factor IX FITC goat IgG Human IF 0.1 mg CL20040F 182 Factor IX HRPO goat IgG Human E, WB 0.2 mg CL20040HP 182 Factor IX/IXa (Calcium Dependent) Purified CaFIX-1 mouse IgG1 Human E, WB 200 μg CL2765AP 259 Factor IX/IXa (Calcium Dependent) Biotin CaFIX-1 mouse IgG1 Human E, WB 100 μg CL2765B 199 Factor V Purified sheep IgG Bovine IP, D 10 mg CL20025A-B 136 Factor V Affinity Purified sheep IgG Bovine WB 0.5 mg CL20025AP-B 249 Factor V HRPO sheep IgG Bovine E 0.2 mg CL20025HP-B 209 Factor V Purified sheep IgG Human IP, N, D, WB 10 mg CL20025A 136 Factor V Affinity Purified sheep IgG Human EC 0.5 mg CL20025AP 317 Factor V Biotin sheep IgG Human E 0.1 mg CL20025B 209 Factor V FITC sheep IgG Human IF 0.1 mg CL20025F 209 Factor V HRPO sheep IgG Human E 0.2 mg CL20025HP 209 Factor VII Purified sheep IgG Human IP, N, D 10 mg CL20030A 136 Factor VII Affinity Purified sheep IgG Human E 0.5 mg CL20030AP 257 Factor VII Biotin sheep IgG Human E 0.1 mg CL20030B 209 Factor VII FITC sheep IgG Human IF 0.1 mg CL20030F 209 Factor VII HRPO sheep IgG Human E 0.2 mg CL20030HP 209 Factor VII/VIIA Purified AA-3 mouse IgG1 Human E, WB 200 μg CL2763AP 259 Factor VII/VIIA Biotin AA-3 mouse IgG1 Human E, WB 100 μg CL2763B 199 Factor VII/VIIa Purified AD-1 mouse IgG1 Human E, WB 200 μg CL2764AP 259 Factor VII/VIIa Biotin AD-1 mouse IgG1 Human E, WB 100 μg CL2764B 199 Factor VII/VIIa (Calcium Dependent) Purified CaFVII-22 mouse IgG1 Human E, WB 200 μg CL2762AP 259 Factor VII/VIIa (Calcium Dependent) Biotin CaFVII-22 mouse IgG1 Human E, WB 100 μg CL2762B 199 Factor VIII.vWF (Non-reactive with rat) Ascites 2F2-A9 mouse IgG1 Human IF, C, P, R 0.5 ml CL1303A 299 Factor VIII:C (Non-reactive with mouse) Purified sheep IgG Human E, IP, N, ID 10 mg CL20035A 136 Factor VIII:C (Non-reactive with mouse) Affinity Purified sheep IgG Human E, N, WB 0.5 mg CL20035AP 317 Factor VIII:C
Load more

Recommended publications
  • An Overview of the Kallikrein Gene Families in Humans and Other Species: Emerging Candidate Tumour Markers૾
    Clinical Biochemistry 36 (2003) 443–452 An overview of the kallikrein gene families in humans and other species: Emerging candidate tumour markers૾ George M. Yousefa,b, Eleftherios P. Diamandisa,b,* aDepartment of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, Ontario, Canada bDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada Abstract Kallikreins are serine proteases with diverse physiologic functions. They are represented by multigene families in many animal species, especially in rat and mouse. Recently, the human kallikrein gene family has been fully characterized and includes 15 members, tandemly localized on chromosome 19q13.4. A new definition has now been proposed for kallikreins, which is not based on function but, rather, on close proximity and structural similarities. In this review, we summarize available information about kallikreins in many animal species with special emphasis on human kallikreins. We discuss the common structural features of kallikreins at the DNA, mRNA and protein levels and overview their evolutionary history. Kallikreins are expressed in a wide range of tissues including the salivary gland, endocrine or endocrine-related tissues such as testis, prostate, breast and endometrium and in the central nervous system. Most, if not all, genes are under steroid hormone regulation. Accumulating evidence indicates that kallikreins are involved in many pathologic conditions. Of special interest is the potential role of kallikreins in the central nervous system. In addition, many kallikreins seem to be candidate tumor markers for many malignancies, especially those of endocrine-related organs. © 2003 The Canadian Society of Clinical Chemists. All rights reserved. Keywords: Kallikrein; Tumor markers; Cancer biomarkers; Prostate cancer; Breast cancer; Ovarian cancer; Alzheimer’s disease; Serine proteases; Chromosome 19; Kallikrein evolution; Rodent kallikreins; Hormonally regulated genes 1.
    [Show full text]
  • Cloning of a New Member of the Human Kallikrein Gene Family, KLK14, Which Is Down-Regulated in Different Malignancies
    [CANCER RESEARCH 61, 3425–3431, April 15, 2001] Cloning of a New Member of the Human Kallikrein Gene Family, KLK14, Which Is Down-Regulated in Different Malignancies George M. Yousef, Angeliki Magklara, Albert Chang, Klaus Jung, Dionyssios Katsaros, and Eleftherios P. Diamandis1 Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada [G. M. Y., A. M., A. C., E. P. D.]; Department of Laboratory Medicine and Pathobiology, University of Toronto, Ontario M5G 1LS, Canada [G. M. Y., A. M., A. C., E. P. D.]; Department of Urology, University Hospital Charite, Humboldt University, Berlin D-10098, Germany [K. J.]; and Department of Gynecologic Oncology, Institute of Obstetrics and Gynecology, University of Turin, Turin 10128, Italy [D. K.] ABSTRACT KLK gene locus and cloned a new gene, KLK14. Here, we describe the cloning of the new gene, its genomic and mRNA structure, its Kallikreins (KLKs) belong to the serine protease family of proteolytic precise location in relation to other known KLKs, and its tissue enzymes. Human pancreatic/renal KLK (KLK1) encodes for an enzyme expression pattern. KLK14 is highly expressed in tissues of the CNS that is involved in posttranslational processing of polypeptide precursors. The function of the other members of this gene family is currently including the brain, cerebellum, and spinal cord. Our preliminary unknown, but growing evidence suggests that many KLKs are implicated results suggest that this gene is down-regulated, at the mRNA level, in in carcinogenesis. By using the positional candidate approach, we were breast, testicular, ovarian, and prostate cancer. able to identify a new human KLK-like gene, KLK14 (also known as KLK-L6).
    [Show full text]
  • Aberrant Human Tissue Kallikrein Levels in the Stratum Corneum and Serum of Patients with Psoriasis: Dependence on Phenotype, Severity and Therapy N
    CLINICAL AND LABORATORY INVESTIGATIONS DOI 10.1111/j.1365-2133.2006.07743.x Aberrant human tissue kallikrein levels in the stratum corneum and serum of patients with psoriasis: dependence on phenotype, severity and therapy N. Komatsu,* à K. Saijoh,§ C. Kuk,* F. Shirasaki,à K. Takeharaà and E.P. Diamandis* *Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5G 1L5, Canada àDepartment of Dermatology and §Department of Hygiene, Graduate School of Medical Science, School of Medicine, Kanazawa University, Kanazawa, Japan Summary Correspondence Background Human tissue kallikreins (KLKs) are a family of 15 trypsin-like or Eleftherios P. Diamandis. chymotrypsin-like secreted serine proteases (KLK1–KLK15). Multiple KLKs have E-mail: [email protected] been quantitatively identified in normal stratum corneum (SC) and sweat as can- didate desquamation-related proteases. Accepted for publication 7 November 2006 Objectives To quantify KLK5, KLK6, KLK7, KLK8, KLK10, KLK11, KLK13 and KLK14 in the SC and serum of patients with psoriasis, and their variation Key words between lesional and nonlesional areas and with phenotype, therapy and severity. diagnostic marker, human kallikreins, psoriasis, The overall SC serine protease activities were also measured. serine proteases, stratum corneum, therapy Methods Enzyme-linked immunosorbent assays and enzymatic assays were used. Conflicts of interest Results The lesional SC of psoriasis generally contained significantly higher levels None declared. of all KLKs. KLK6, KLK10 and KLK13 levels were significantly elevated even in the nonlesional SC. The overall trypsin-like, plasmin-like and furin-like activities were significantly elevated in the lesional SC.
    [Show full text]
  • Human Tissue Kallikrein Expression in the Stratum Corneum and Serum of Atopic Dermatitis Patients
    DOI:10.1111/j.1600-0625.2007.00562.x www.blackwellpublishing.com/EXD Original Article Human tissue kallikrein expression in the stratum corneum and serum of atopic dermatitis patients Nahoko Komatsu1,2,3,4, Kiyofumi Saijoh4, Cynthia Kuk1, Amber C. Liu1, Saba Khan1, Fumiaki Shirasaki3, Kazuhiko Takehara3 and Eleftherios P. Diamandis1,2 1Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, ON, Canada; 2Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada; 3Department of Dermatology, Graduate School of Medical Science, School of Medicine, Kanazawa University, Kanazawa, Japan; 4Department of Hygiene, Graduate School of Medical Science, School of Medicine, Kanazawa University, Kanazawa, Japan Correspondence: Eleftherios P. Diamandis, MD, PhD, FRCPC, Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 600 University Avenue, Toronto, ON M5G 1X5, Canada, Tel.: +1 416 586 8443, Fax: +1 416 586 8628, e-mail: [email protected] Accepted for publication 9 March 2007 Abstract: Human tissue kallikreins are a family of 15 trypsin- or differ significantly. In the serum of AD patients, KLK8 was chymotrypsin-like secreted serine proteases (KLK1–KLK15). Many significantly elevated and KLK5 and KLK11 were significantly KLKs have been identified in normal stratum corneum (SC) and decreased. However, their serum levels were not modified by sweat, and are candidate desquamation-related proteases. We corticosteroid topical agents. The alterations of KLK levels in the report quantification by enzyme-linked immunosorbent assay SC of AD were more pronounced than those in the serum. KLK7 (ELISA) of KLK5, KLK6, KLK7, KLK8, KLK10, KLK11, KLK13 and in the serum was significantly correlated with eosinophil counts in KLK14 in the SC and serum of atopic dermatitis (AD) patients by the blood of AD patients, while KLK5, KLK8 and KLK11 were ELISA, and examine their variation with clinical phenotype, significantly correlated with LDH in the serum.
    [Show full text]
  • SA1 Oxygen Binding Heme Proteins
    8P Research Symposium transcriptional and post-translational responses to hypoxia are SA1 not fully understood. Our model proposes that mitochondria function as cellular oxygen sensors through a process that Oxygen binding heme proteins involves interaction of molecular oxygen with Complex III of M.T. Wilson the electron transport chain. Hypoxia results in a paradoxical increase in the release of reactive oxygen species from the outer Biological Sciences, University of Essex, Colchester, UK surface of the inner mitochondrial membrane. These signaling Myoglobin (Mb) and Hemoglobin (Hb), the respiratory pig- levels of oxidant stress lead to the activation of transcription fac- ments of mammals and some molluscs, annelids and arthro- tors including Hypoxia-Inducible Factor (HIF-1 and HIF-2) and pods, belong to an ancient super-family of heme associated glo- NF-kB, and they trigger cell-specific post-translational responses bin proteins. Members of this family share common structural to hypoxia. Stabilization of HIF-α protein in hypoxia is abro- and spectral features. They also share some general functional gated when genetic modifications to the electron transport chain characteristics such as the ability to bind ligands, e.g. O2, CO and lead to loss-of-function in terms of the ability to generate ROS NO, at the iron atom and to undergo redox changes. These prop- signals during hypoxia. Conversely, genetic modifications to erties are used in vivo to perform a wide range of biochemical Complex II that induce a chronic increase in mitochondrial ROS and physiological roles. production lead to the stabilization of HIF-α under normoxic While it is acknowledged that the major role of Hb is to bind conditions.
    [Show full text]
  • Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
    Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................
    [Show full text]
  • Download, Or Email Articles for Individual Use
    Florida State University Libraries Faculty Publications The Department of Biomedical Sciences 2010 Functional Intersection of the Kallikrein- Related Peptidases (KLKs) and Thrombostasis Axis Michael Blaber, Hyesook Yoon, Maria Juliano, Isobel Scarisbrick, and Sachiko Blaber Follow this and additional works at the FSU Digital Library. For more information, please contact [email protected] Article in press - uncorrected proof Biol. Chem., Vol. 391, pp. 311–320, April 2010 • Copyright ᮊ by Walter de Gruyter • Berlin • New York. DOI 10.1515/BC.2010.024 Review Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis Michael Blaber1,*, Hyesook Yoon1, Maria A. locus (Gan et al., 2000; Harvey et al., 2000; Yousef et al., Juliano2, Isobel A. Scarisbrick3 and Sachiko I. 2000), as well as the adoption of a commonly accepted Blaber1 nomenclature (Lundwall et al., 2006), resolved these two fundamental issues. The vast body of work has associated 1 Department of Biomedical Sciences, Florida State several cancer pathologies with differential regulation or University, Tallahassee, FL 32306-4300, USA expression of individual members of the KLK family, and 2 Department of Biophysics, Escola Paulista de Medicina, has served to elevate the importance of the KLKs in serious Universidade Federal de Sao Paulo, Rua Tres de Maio 100, human disease and their diagnosis (Diamandis et al., 2000; 04044-20 Sao Paulo, Brazil Diamandis and Yousef, 2001; Yousef and Diamandis, 2001, 3 Program for Molecular Neuroscience and Departments of 2003;
    [Show full text]
  • Induction of Complement C3a Receptor Responses by Kallikrein-Related Peptidase 14
    The Journal of Immunology Induction of Complement C3a Receptor Responses by Kallikrein-Related Peptidase 14 Katerina Oikonomopoulou,* Robert A. DeAngelis,* Hui Chen,* Eleftherios P. Diamandis,†,‡ Morley D. Hollenberg,x,{ Daniel Ricklin,*,1 and John D. Lambris*,1 Activation of the complement system is primarily initiated by pathogen- and damage-associated molecular patterns on cellular surfaces. However, there is increasing evidence for direct activation of individual complement components by extrinsic proteinases as part of an intricate crosstalk between physiological effector systems. We hypothesized that kallikrein-related peptidases (KLKs), previously known to regulate inflammation via proteinase-activated receptors, can also play a substantial role in innate immune responses via complement. Indeed, KLKs exemplified by KLK14 were efficiently able to cleave C3, the point of convergence of the complement cascade, indicating a potential modulation of C3-mediated functions. By using in vitro fragmentation assays, mass spectrometric analysis, and cell signaling measurements, we pinpointed the generation of the C3a fragment of C3 as a product Downloaded from with potential biological activity released by the proteolytic action of KLK14. Using mice with various complement deficiencies, we demonstrated that the intraplantar administration of KLK14 results in C3-associated paw edema. The edema response was dependent on the presence of the receptor for C3a but was not associated with the receptor for the downstream complement effector C5a. Our findings point to C3 as one of the potential substrates of KLKs during inflammation. Given the wide distribution of the KLKs in tissues and biological fluids where complement components may also be expressed, we suggest that via C3 processing, tissue-localized KLKs can play an extrinsic complement-related role during activation of the innate immune response.
    [Show full text]
  • Effects of Kallikrein-Related Peptidase 14 Gene Inhibition by Small Interfering RNA in Ovarian Carcinoma Cells
    256 MOLECULAR MEDICINE REPORTS 5: 256-259, 2012 Effects of kallikrein-related peptidase 14 gene inhibition by small interfering RNA in ovarian carcinoma cells RUITAO ZHANG, HUIRONG SHI, ZHIMIN CHEN, WEI FENG, HAILING ZHANG and KAIYUAN WU Department of Obstetrics and Gynaecology, First Affiliated Hospital, Zhengzhou University, Zhengzhou 450052, P.R. China Received July 24, 2011; Accepted September 30, 2011 DOI: 10.3892/mmr.2011.625 Abstract. Kallikrein-related peptidase 14 (KLK14) is a member Moreover, more than 70% of ovarian cancer patients are found of the tissue kallikrein family of proteases, which are associated to present with late-stage disease at the initial diagnosis (1). with the pathogenesis of malignant tumors and are over expressed KLK14, also known as kallikrein-like protein 6, was found in ovarian carcinoma. However, the mechanism through which to be overexpressed in various malignant epithelial tissues KLK14 is implicated in ovarian cancer remains unclear. The and biological fluids, particularly in steroid hormone-related aim of the present study was to investigate the effects of malignancies, including breast cancer, ovarian carcinoma KLK14 gene inhibition by small interfering RNA (siRNA) and prostate cancer (2-4). Abnormal expression of KLK14 on the growth, apoptosis and invasion of ovarian carcinoma was found to be related with poor prognosis and has been cells in vitro. KLK14 siRNA was transiently transfected into demonstrated to be a potential biomarker for these malignan- SK-OV-3 and OVCAR-3 ovarian carcinoma cells for 48 h. The cies (4,5). However, the mechanism through which KLK14 is expression of KLK14 was determined by reverse transcription- implicated in ovarian carcinoma remains unclear.
    [Show full text]
  • Activation Profiles and Regulatory Cascades of the Human Kallikrein-Related Peptidases Hyesook Yoon
    Florida State University Libraries Electronic Theses, Treatises and Dissertations The Graduate School 2008 Activation Profiles and Regulatory Cascades of the Human Kallikrein-Related Peptidases Hyesook Yoon Follow this and additional works at the FSU Digital Library. For more information, please contact [email protected] FLORIDA STATE UNIVERSITY COLLEGE OF ARTS AND SCIENCES ACTIVATION PROFILES AND REGULATORY CASCADES OF THE HUMAN KALLIKREIN-RELATED PEPTIDASES By HYESOOK YOON A Dissertation submitted to the Department of Chemistry and Biochemistry in partial fulfillment of the requirements for the degree of Doctor of Philosophy Degree Awarded: Fall Semester, 2008 The members of the Committee approve the dissertation of Hyesook Yoon defended on July 10th, 2008. ________________________ Michael Blaber Professor Directing Dissertation ________________________ Hengli Tang Outside Committee Member ________________________ Brian Miller Committee Member ________________________ Oliver Steinbock Committee Member Approved: ____________________________________________________________ Joseph B. Schlenoff, Chair, Department of Chemistry and Biochemistry The Office of Graduate Studies has verified and approved the above named committee members. ii ACKNOWLEDGMENTS I would like to dedicate this dissertation to my parents for all your support, and my sister and brother. I would also like to give great thank my advisor, Dr. Blaber for his patience, guidance. Without him, I could never make this achievement. I would like to thank to all the members in Blaber lab. They are just like family to me and I deeply appreciate their kindness, consideration and supports. I specially like to thank to Mrs. Sachiko Blaber for her endless guidance and encouragement. I would like to thank Dr Jihun Lee, Margaret Seavy, Rani and Doris Terry for helpful discussions and supports.
    [Show full text]
  • A Multiparametric Serum Kallikrein Panel for Diagnosis of Non ^ Small
    Imaging, Diagnosis, Prognosis A Multiparametric Serum Kallikrein Panel for Diagnosis of Non ^ Small Cell Lung Carcinoma Chris Planque,1, 2 Lin Li,3 Yingye Zheng,3 Antoninus Soosaipillai,1, 2 Karen Reckamp,4 David Chia,5 Eleftherios P. Diamandis,1, 2 and Lee Goodglick5 Abstract Purpose: Human tissue kallikreins are a family of15 secreted serine proteases.We have previous- ly shown that the expression of several tissue kallikreins is significantly altered at the transcription- al level in lung cancer. Here, we examined the clinical value of 11members of the tissue kallikrein family as potential biomarkers for lung cancer diagnosis. Experimental Design: Serum specimens from 51 patients with non ^ small cell lung cancer (NSCLC) and from 50 healthy volunteers were collected. Samples were analyzed for11kallikreins (KLK1, KLK4-8, and KLK10-14) by specific ELISA. Data were statistically compared and receiver operating characteristic curves were constructed for each kallikrein and for various combinations. Results: Compared with sera from normal subjects, sera of patients with NSCLC had lower levels of KLK5, KLK7, KLK8, KLK10, and KLK12, and higher levels of KLK11, KLK13, and KLK14. Expres- sion of KLK11and KLK12 was positively correlated with stage.With the exception of KLK5, expres- sion of kallikreins was independent of smoking status and gender. KLK11, KLK12, KLK13, and KLK14 were associated with higher risk of NSCLC as determined by univariate analysis and con- firmed by multivariate analysis.The receiver operating characteristic curve of KLK4, KLK8, KLK10, KLK11,KLK12, KLK13, and KLK14 combined exhibited an area under the curve of 0.90 (95% con- fidence interval, 0.87-0.97).
    [Show full text]
  • Is Generation of C3(H2O) Necessary for Activation of the Alternative Pathway T in Real Life? ⁎ Kristina N
    Molecular Immunology 114 (2019) 353–361 Contents lists available at ScienceDirect Molecular Immunology journal homepage: www.elsevier.com/locate/molimm Is generation of C3(H2O) necessary for activation of the alternative pathway T in real life? ⁎ Kristina N. Ekdahla,b, , Camilla Mohlinb, Anna Adlera, Amanda Åmana, Vivek Anand Manivela, Kerstin Sandholmb, Markus Huber-Langc, Karin Fromella, Bo Nilssona a Department of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala, Sweden b Linnaeus Center of Biomaterials Chemistry, Linnaeus University, Kalmar, Sweden c Institute for Clinical and Experimental Trauma Immunology, University Hospital of Ulm, Ulm, Germany ARTICLE INFO ABSTRACT Keywords: In the alternative pathway (AP) an amplification loop is formed, which is strictly controlled by various fluid- Complement system phase and cell-bound regulators resulting in a state of homeostasis. Generation of the “C3b-like” C3(H2O) has C3(H2O) been described as essential for AP activation, since it conveniently explains how the initial fluid-phase AP Conformation convertase of the amplification loop is generated. Also, the AP has a status of being an unspecific pathway Analysis despite thorough regulation at different surfaces. Proteases During complement attack in pathological conditions and inflammation, large amounts of C3b are formed by Alternative pathway the classical/lectin pathway (CP/LP) convertases. After the discovery of LP´s recognition molecules and its tight interaction with the AP, it is increasingly likely that the AP acts in vivo mainly as a powerful amplification mechanism of complement activation that is triggered by previously generated C3b molecules initiated by the binding of specific recognition molecules. Also in many pathological conditions caused by a dysregulated AP amplification loop such as paroxysmal nocturnal hemoglobulinuria (PNH) and atypical hemolytic uremic syndrome (aHUS), C3b is available due to minute LP and CP activation and/or generated by non-complement proteases.
    [Show full text]