The Effect of Angiotensin Receptor
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Datasheet: MCA2736GA Product Details
Datasheet: MCA2736GA Description: MOUSE ANTI HUMAN MMP-9 ACTIVATED Specificity: MMP-9 ACTIVATED Other names: GELATINASE B Format: Purified Product Type: Monoclonal Antibody Clone: 4A3 Isotype: IgG1 Quantity: 0.1 mg Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Flow Cytometry Immunohistology - Frozen Immunohistology - Paraffin 1/25 - 1/100 ELISA Immunoprecipitation Western Blotting Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls. Target Species Human Product Form Purified IgG - liquid Preparation Purified IgG prepared by affinity chromatography on Protein G Buffer Solution Phosphate buffered saline Preservative 0.09% Sodium Azide (NaN3) Stabilisers Approx. Protein IgG concentration 0.5mg/ml Concentrations Immunogen Ovalbumin conjugated synthetic peptide corresponding to a region within the N-terminus of human MMP-9. Page 1 of 3 External Database Links UniProt: P14780 Related reagents Entrez Gene: 4318 MMP9 Related reagents Synonyms CLG4B Fusion Partners Spleen cells from immunised Balb/c mice were fused with cells of the Ag8563 myeloma cell line. Specificity Mouse anti Human MMP-9 Activated antibody, clone 4A3 recognizes the active form of human matrix metalloproteinase 9 (MMP9). -
Serum Level of Cathepsin B and Its Density in Men with Prostate Cancer As Novel Markers of Disease Progression
ANTICANCER RESEARCH 24: 2573-2578 (2004) Serum Level of Cathepsin B and its Density in Men with Prostate Cancer as Novel Markers of Disease Progression HIDEAKI MIYAKE1, ISAO HARA2 and HIROSHI ETO1 1Department of Urology, Hyogo Medical Center for Adults, 13-70 Kitaohji-cho, Akashi; 2Department of Urology, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Kobe, Japan Abstract. Background: Cathepsin B has been shown to play in men in Western industrialized countries and is the second an important role in invasion and metastasis of prostate leading cause of cancer-related death (1). Recent cancer. The objective of this study was to determine whether progression in the fields of diagnosis and follow-up using serum levels of cathepsin B and its density (cathepsin B-D) prostate-specific antigen (PSA) and its associated could be used as predictors of disease extension as well as parameters have contributed to early detection and accurate prognosis in patients with prostate cancer. Materials and prediction of prognosis (2, 3). However, despite these Methods: Serum levels of cathepsin B in 60 healthy controls, advances, more than 50% of patients still show evidence of 80 patients with benign prostatic hypertrophy (BPH) and 120 advanced disease at the time of diagnosis, and the currently patients with prostate cancer were measured by a sandwich available parameters are not correlated with the clinical enzyme immunoassay. Cathepsin B-D was calculated by course in some patients during progression to hormone- dividing the serum levels of cathepsin B by the prostate refractory disease (4); hence, there is a pressing need to volume, which was measured using transrectal ultra- develop a novel diagnostic and monitoring marker system sonography. -
And Peptide Sequences (>95 % Confidence) in the Non-Raft Fraction
Supplementary Table 1: Protein identities, their probability scores (protein score and expect score) and peptide sequences (>95 % confidence) in the non-raft fraction. Protein name Protein score Expect score Peptide sequences Glial fibrillary acidic protein 97 0.000058 LALDIEIATYR 0.0000026 LALDIEIATYR Phosphatidylinositol 3-kinase 25 0.038 HGDDLR Uveal autoantigen with coiled-coil domains and ankyrin repeats protein 30 0.03 TEELNR ADAM metallopeptidase domain 32 347 0.0072 SGSICDK 0.0059 YTFCPWR 0.00028 CSEVGPYINR 0.0073 DSASVIYAFVR 0.00044 DSASVIYAFVR 0.00047 LICTYPLQTPFLR 0.0039 LICTYPLQTPFLR 0.001 LICTYPLQTPFLR 0.0000038 AYCFDGGCQDIDAR 0.00000043 AYCFDGGCQDIDAR 0.0000042 VNQCSAQCGGNGVCTSR 0.0000048 NAPFACYEEIQSQTDR 0.000019 NAPFACYEEIQSQTDR Alpha-fetoprotein 24 0.0093 YIYEIAR Junction plakoglobin 214 0.011 ATIGLIR 0.0038 LVQLLVK 0.000043 EGLLAIFK 0.00027 QEGLESVLK 0.000085 TMQNTSDLDTAR 0.000046 ALMGSPQLVAAVVR 0.01 LLNQPNQWPLVK 0.01 NEGTATYAAAVLFR 0.004 NLALCPANHAPLQEAAVIPR 0.0007 VLSVCPSNKPAIVEAGGMQALGK 0.00086 ILVNQLSVDDVNVLTCATGTLSNLTCNNSK Catenin beta-1 54 0.000043 EGLLAIFK Lysozyme 89 0.0026 STDYGIFQINSR 0.00051 STDYGIFQINSR 1 0.0000052 STDYGIFQINSR Annexin A2 72 0.0036 QDIAFAYQR 72 0.0000043 TNQELQEINR Actin, cytoplasmic 61 0.023 IIAPPER 0.021 IIAPPER 0.0044 AGFAGDDAPR 0.013 EITALAPSTMK 0.0013 LCYVALDFEQEMATAASSSSLEK 0.023 IIAPPER 0.021 IIAPPER 0.0044 AGFAGDDAPR 0.0013 LCYVALDFEQEMATAASSSSLEK 0.023 IIAPPER 0.021 IIAPPER 0.0044 AGFAGDDAPR 0.013 EITALAPSTMK ACTA2 protein 35 0.0044 AGFAGDDAPR 0.013 EITALAPSTMK Similar to beta actin -
Pathophysiology of Thrombotic Thrombocytopenic Purpura and Hemolytic Uremic Syndrome
Pathophysiology of thrombotic thrombocytopenic purpura and hemolytic uremic syndrome Johanna A. Kremer Hovinga*†, Silvan R. Heeb *†, Magdalena Skowronska*† and Monica Schaller *† *Department of Hematology and Central Hematology Laboratory, Inselspital, Bern University Hospital, Bern, and †Department for BioMedical Research, University of Bern, Bern, Switzerland Abstract: 120 Text: 4997 References: 100 Tables: 1 Figures: 1 Correspondence to: Johanna A. Kremer Hovinga, MD Department of Hematology and Central Hematology Laboratory Inselspital, Bern University Hospital CH-3010 Bern, Switzerland Phone: +41 31 632 02 65 Fax: +41 31 632 18 82 e-mail: [email protected] 1 Summary Thrombotic microangiopathies are rare disorders characterized by the concomitant occurrence of severe thrombocytopenia, microangiopathic hemolytic anemia, and a variable degree of ischemic end organ damage. The latter particularly affects the brain, the heart and the kidneys. The primary forms, thrombotic thrombocytopenic purpura (TTP) and hemolytic uremic syndrome (HUS), although in their clinical presentation often overlapping, have distinctive pathophysiologies. TTP is the consequence of a severe ADAMTS13 deficiency, immune- mediated due to circulating autoantibodies (iTTP), or caused by mutations in the ADAMTS13 gene (cTTP). HUS develops following an infection with Shiga-toxin producing bacteria (STEC-HUS), or as the result of excessive activation of the alternative pathway of the complement system because of mutations in genes of complement system proteins in atypical HUS (aHUS). Key words Thrombotic Thrombocytopenic Purpura; Hemolytic Uremic Syndrome; ADAMTS13; Alternative Complement Pathway; Shiga Toxin 2 Introduction Thrombotic thrombocytopenic purpura (TTP) and hemolytic uremic syndrome (HUS) are acute thrombotic microangiopathies (TMA), characterized by acute episodes of intravascular hemolysis, thrombocytopenia and microvascular thrombosis leading to end organ damage becoming apparent as acute kidney injury, cerebrovascular accidents or seizures, and myocardial infarction [1, 2]. -
MMP-2 and MMP-9 Are Prominent Matrix Metalloproteinases During Atherosclerosis Development in the Ldlr-/-Apob100/100 Mouse
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE 28: 247-253, 2011 MMP-2 and MMP-9 are prominent matrix metalloproteinases during atherosclerosis development in the Ldlr-/-Apob100/100 mouse DICK WÅGSÄTER1, CHAOYONG ZHU1, JOHAN BJÖRKEGREN2, JOSEFIN SKOGSBERG2 and PER ERIKSSON1 1Atherosclerosis Research Unit, Center for Molecular Medicine, Department of Medicine and 2The Cardiovascular Genomics Group, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Solna, Stockholm, Sweden Received February 9, 2011; Accepted March 23, 2011 DOI: 10.3892/ijmm.2011.693 Abstract. Matrix-degrading proteases capable of degrading atherosclerotic plaque formation. Matrix metalloproteinases components of the extracellular matrix may play an important (MMPs) are a large family of proteases that can degrade all role in development and progression of atherosclerotic lesions. components of the ECM. MMPs are highly expressed in In the present study, we used the Ldlr-/-Apob100/100 mouse atherosclerotic plaques and perturbed proteolytic activity has model, which has a plasma lipoprotein profile similar to that been implicated in atherogenesis and the precipitation of acute of humans with atherosclerosis, to study the expression of coronary syndromes. matrix metalloproteinases (MMPs) during early stages of Studies in mice have suggested that different members of atherosclerosis development. We analyzed the expression of the MMP family may exert divergent effects during the 11 proteases and three protease inhibitors in 5- to 40-week-old atherosclerotic process (2). MMPs are proposed to enhance Ldlr-/-Apob100/100 mice. Expression and activity of MMP-2 and migration and proliferation of smooth muscle and inflammatory MMP-9 was increased in advanced atherosclerotic lesions cells during early stages of the atherosclerotic process. -
WO 2016/110768 Al 14 July 2016 (14.07.2016) W P O PCT
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2016/110768 Al 14 July 2016 (14.07.2016) W P O PCT (51) International Patent Classification: Rue de la Blancherie 11, 1022 Chavannes-pres-Renens A61K 35/74 (2015.01) A61P 25/28 (2006.01) (CH). HANNA, Walid; Avenue des Bains 40, 1007 Lausanne (CH). FAK, Frida; Qvantenborgsvagen 4B, 227 (21) International Application Number: 38 Lund (SE). MARUNGRUANG, Nittaya; Ostra Varvs- PCT/IB2015/059945 gatan 20A, 2 11 75 Malmo (SE). (22) International Filing Date: (74) Agent: ROLAND, Andre; c/o ANDRE ROLAND S.A., 23 December 2015 (23. 12.2015) P.O. Box 5107, 1002 Lausanne (CH). (25) Filing Language: English (81) Designated States (unless otherwise indicated, for every (26) Publication Language: English kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (30) Priority Data: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, PCT/IB20 15/050 127 DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, 7 January 2015 (07.01 .2015) IB HN, HR, HU, ID, IL, ΓΝ , IR, IS, JP, KE, KG, KN, KP, KR, PCT/IB2015/053957 27 May 2015 (27.05.2015) IB KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, (71) Applicant: ECOLE POLYTECHNIQUE FEDERALE MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, DE LAUSANNE (EPFL) [CH/CH]; EPFL-TTO, EPFL PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, SC, Innovation Park J, 1015 Lausanne (CH). -
Microglial Dysfunction and Defectiveя-Amyloid Clearance Pathways In
8354 • The Journal of Neuroscience, August 13, 2008 • 28(33):8354–8360 Neurobiology of Disease Microglial Dysfunction and Defective -Amyloid Clearance Pathways in Aging Alzheimer’s Disease Mice Suzanne E. Hickman,1 Elizabeth K. Allison,1 and Joseph El Khoury1,2 1Center for Immunology and Inflammatory Diseases, Division of Rheumatology, Allergy, and Immunology, and 2Division of Infectious Diseases, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129 Early microglial accumulation in Alzheimer’s disease (AD) delays disease progression by promoting clearance of -amyloid (A) before formation of senile plaques. However, persistent A accumulation despite increasing microglial numbers suggests that the ability of microglia to clear A may decrease with age and progression of AD pathology. To determine the effects of aging and A deposition on microglial ability to clear A, we used quantitative PCR to analyze gene expression in freshly isolated adult microglia from 1.5-, 3-, 8-, and 14-month-old transgenic PS1-APP mice, an established mouse model of AD, and from their nontransgenic littermates. We found that microglia from old PS1-APP mice, but not from younger mice, have a twofold to fivefold decrease in expression of the A-binding scavenger receptors scavenger receptor A (SRA), CD36, and RAGE (receptor for advanced-glycosylation endproducts), and the A- degrading enzymes insulysin, neprilysin, and MMP9, compared with their littermate controls. In contrast, PS1-APP microglia had a 2.5-fold increase in the proinflammatory cytokines IL-1 (interleukin-1) and tumor necrosis factor ␣ (TNF␣), suggesting that there is an inverse correlation between cytokine production and A clearance. In support of this possibility, we found that incubation of cultured N9 mouse microglia with TNF␣ decreased the expression of SRA and CD36 and reduced A uptake. -
Correlation Between Human Epidermal
Gynecologic Oncology 99 (2005) 415 – 421 www.elsevier.com/locate/ygyno Correlation between human epidermal growth factor receptor family (EGFR, HER2, HER3, HER4), phosphorylated Akt (P-Akt), and clinical outcomes after radiation therapy in carcinoma of the cervixi Christopher M. Lee a, Dennis C. Shrieve a, Karen A. Zempolich b, R. Jeffrey Lee c, Elizabeth Hammond d, Diana L. Handrahan e, David K. Gaffney a,* a Department of Radiation Oncology, Huntsman Cancer Hospital and University of Utah Medical Center, 1950 Circle of Hope, Salt Lake City, UT 84112, USA b Department of Gynecologic Oncology, University of Utah Medical Center, Salt Lake City, UT 84112, USA c Department of Radiation Oncology, LDS Hospital, Salt Lake City, UT 84143, USA d Department of Pathology, LDS Hospital, Salt Lake City, UT 84143, USA e Statistical Data Center, LDS Hospital, Salt Lake City, UT 84143, USA Received 13 January 2005 Available online 12 September 2005 Abstract Objective. To investigate prognostic significance of and correlations between HER1 (EGFR), HER2 (c-erb-B2), HER3 (c-erb-B3), HER4 (c- erb-B4), and phosphorylated Akt (P-Akt) in patients treated with radiation for cervical carcinoma. Methods. Fifty-five patients with stages I–IVA cervical carcinoma were treated with definitive radiotherapy. Tumor expression of each biomarker was quantitatively scored by an automated immunohistochemical imaging system. Parametric correlations were performed between biomarkers. Univariate and multivariate analysis was performed with disease-free survival (DFS) and overall survival (OS) as primary endpoints. Results. Correlations were observed between expression of HER2 and HER4 (P = 0.003), and HER3 and HER4 (P = 0.004). -
MMP9 / Gelatinase B Antibody (Internal) Rabbit Polyclonal Antibody Catalog # ALS12805
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 MMP9 / Gelatinase B Antibody (Internal) Rabbit Polyclonal Antibody Catalog # ALS12805 Specification MMP9 / Gelatinase B Antibody (Internal) - Product Information Application IHC Primary Accession P14780 Reactivity Human, Guinea Pig Host Rabbit Clonality Polyclonal Calculated MW 78kDa KDa MMP9 / Gelatinase B Antibody (Internal) - Additional Information Gene ID 4318 Anti-MMP-9 antibody IHC of human spleen. Other Names Matrix metalloproteinase-9, MMP-9, MMP9 / Gelatinase B Antibody (Internal) - 3.4.24.35, 92 kDa gelatinase, 92 kDa type Background IV collagenase, Gelatinase B, GELB, 67 kDa matrix metalloproteinase-9, 82 kDa matrix May play an essential role in local proteolysis metalloproteinase-9, MMP9, CLG4B of the extracellular matrix and in leukocyte migration. Could play a role in bone Target/Specificity osteoclastic resorption. Cleaves KiSS1 at a Recognizes pro (latent) and activated forms Gly-|-Leu bond. Cleaves type IV and type V of human MMP-9 at 92kD and ~86kD, collagen into large C-terminal three quarter respectively. Shows no cross-reaction with fragments and shorter N-terminal one quarter pro and active forms of other MMPs. fragments. Degrades fibronectin but not laminin or Pz-peptide. Reconstitution & Storage Long term: Add glycerol (40-50%) -20°C; MMP9 / Gelatinase B Antibody (Internal) - Short term: +4°C References Precautions MMP9 / Gelatinase B Antibody (Internal) is Wilhelm S.M.,et al.J. Biol. Chem. for research use only and not for use in 264:17213-17221(1989). diagnostic or therapeutic procedures. Huhtala P.,et al.J. Biol. Chem. 266:16485-16490(1991). -
Gene Polymorphisms and Circulating Levels of MMP-2 and MMP-9
ANTICANCER RESEARCH 40 : 3619-3631 (2020) doi:10.21873/anticanres.14351 Review Gene Polymorphisms and Circulating Levels of MMP-2 and MMP-9: A Review of Their Role in Breast Cancer Risk SUÉLÈNE GEORGINA DOFARA 1,2,3 , SUE-LING CHANG 1,2 and CAROLINE DIORIO 1,2,3 1Division of Oncology, CHU de Québec-Université Laval Research Center, Quebec City, QC, Canada; 2Cancer Research Center – Laval University, Quebec City, QC, Canada; 3Department of Social and Preventive Medicine, Faculty of Medicine, Laval University, Quebec City, QC, Canada Abstract. MMP-2 and MMP-9 genes have been suggested to (4), as well as other extracellular matrix components, thus play a role in breast cancer. Their functions have been promoting extracellular matrix remodeling and consequently associated with invasion and metastasis of breast cancer; play a key role in several physiological processes, such as however, their involvement in the development of the disease is tissue repair, wound healing, and cell differentiation (5, 6). not well-established. Herein, we reviewed the literature Gelatinases could be involved in carcinogenesis processes, investigating the association between circulating levels and including cell proliferation, angiogenesis, and tumor metastasis polymorphisms of MMP-2 and MMP-9 and breast cancer risk. through their proteolytic function (7). Indeed, the literature Various studies report conflicting results regarding the suggests their involvement in several pathological processes relationship of polymorphisms in MMP-2 and MMP-9 and critical for cancer development, including inflammation, breast cancer risk. Nevertheless, it appears that the T allele in angiogenesis, and cell proliferation, as well as in tumor rs243865 and rs2285053 in MMP-2 are associated with progression (8, 9). -
Proteomic Identification of in Vivo Substrates for Matrix
Proteomic Identification of In Vivo Substrates for Matrix Metalloproteinases 2 and 9 Reveals a Mechanism for Resolution of Inflammation This information is current as of September 23, 2021. Kendra J. Greenlee, David B. Corry, David A. Engler, Risë K. Matsunami, Philippe Tessier, Richard G. Cook, Zena Werb and Farrah Kheradmand J Immunol 2006; 177:7312-7321; ; doi: 10.4049/jimmunol.177.10.7312 Downloaded from http://www.jimmunol.org/content/177/10/7312 References This article cites 48 articles, 14 of which you can access for free at: http://www.jimmunol.org/ http://www.jimmunol.org/content/177/10/7312.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on September 23, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2006 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Proteomic Identification of In Vivo Substrates for Matrix Metalloproteinases 2 and 9 Reveals a Mechanism for Resolution of Inflammation1 Kendra J. Greenlee,* David B. -
Protein Expression Profiles in Pancreatic Adenocarcinoma
[CANCER RESEARCH 64, 9018–9026, December 15, 2004] Protein Expression Profiles in Pancreatic Adenocarcinoma Compared with Normal Pancreatic Tissue and Tissue Affected by Pancreatitis as Detected by Two- Dimensional Gel Electrophoresis and Mass Spectrometry Jianjun Shen,1 Maria D. Person,2 Jijiang Zhu,3 James L. Abbruzzese,3 and Donghui Li3 1Department of Carcinogenesis, Science Park-Research Division, The University of Texas M. D. Anderson Cancer Center, Smithville, Texas; 2Division of Pharmacology and Toxicology, The University of Texas, Austin, Texas; and 3Department of Gastrointestinal Medical Oncology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas ABSTRACT revealed a large number of differentially expressed genes but little overlap of identified genes among various gene expression ap- Pancreatic cancer is a rapidly fatal disease, and there is an urgent need proaches. Furthermore, although genetic mutation and/or errant gene for early detection markers and novel therapeutic targets. The current expression may underlie a disease, the biochemical bases for most study has used a proteomic approach of two-dimensional (2D) gel elec- trophoresis and mass spectrometry (MS) to identify differentially ex- diseases are caused by protein defects. Therefore, profiling differen- pressed proteins in six cases of pancreatic adenocarcinoma, two normal tially expressed proteins is perhaps the most important and useful adjacent tissues, seven cases of pancreatitis, and six normal pancreatic approach in development of diagnostic screening and therapeutic tissues. Protein extracts of individual sample and pooled samples of each techniques. type of tissues were separated on 2D gels using two different pH ranges. The proteomic approach has offered many opportunities and chal- Differentially expressed protein spots were in-gel digested and identified lenges in identifying new tumor markers and therapeutic targets and in by MS.