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MAB13415 Anti-MMP-9 Antibody, clone GE-213

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      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      HIP, WB, IHC, FUNCMPurifiedMonoclonal Antibody
      Catalogue NumberMAB13415
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-MMP-9 Antibody, clone GE-213
      Alternate Names
      • Gelatinase B
      • 92 kDa Type IV Collagenase
      Product Information
      • POSITIVE CONTROL: Cytotrophoblastic columns, the endothelial and fibroblastic stromal cells of villi, and the large decidualized cells of decidual membrane in placenta (Hurskainen et al., 1996). Macrophages in arteries (Nikkari et al., 1996), and fibroblast, endothelial, and tumor cells in breast carcinomas (Soini et al., 1994; Visscher et al., 1994). Conditioned serum-free medium from (dexamethasone-treated) human fibrosarcoma HT-10801 (Nikkari et al., 1996) or endothelial HUVEC4 (Schnaper et al., 1993) cells.
      PresentationPurified from ascites fluid by Protein G chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 0.09% sodium azide.
      Quality LevelMQ100
      ApplicationAnti-MMP-9 Antibody, clone GE-213 is an antibody against MMP-9 for use in IP, WB & IH.
      Key Applications
      • Immunoprecipitation
      • Western Blotting
      • Immunohistochemistry
      • Affects Function
      Application NotesWestern Blotting (non-reducing; Nikkari et al., 1996) (Use Ab at 1μg/mL for 2hrs at RT)

      Immunohistochemistry (Acetone-fixed frozen; Hurskainen, 1996): 1:100 for 30 minutes at room temperature

      Immunoprecipitation: 2-5 μg/mg protein lysate (use protein G to precipitate immune complex).

      Inhibition of MMP-9 Activity: 2-4μg/mL (Visscher, 1994)

      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenPurified human gelatinase B.
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificityUnder non-reducing conditions, it recognizes proteins of 92 kDa and 86 kDa which are identified as pro (latent) and active forms of matrix metalloproteinase-9 (MMP-9; also known as 92 kDa and collagenase IV or gelatinase B) of human MMP-9. MAB13415 reacts with the complex (~200 kDa) of MMP-9 and tissue inhibitor of metalloproteinases-1 (TIMP-1; Nikkari et al., 1996). It shows no cross-reaction with pro and active forms of MMP-2 (Nikkari et al., 1996). Clone GE-213 also shows very low reactivity to mouse MMP-9 proteins by western blot, but at high enough antibody and antigen concentrations some detection is possible. Mouse immunhistochemistry is untested. Cellular Localization: Peripheral cytoplasmic.
      Species Reactivity
      • Human
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryProteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
      Gene Symbol
      • MMP9
      • MMP-9
      • GELB
      • CLG4B
      • EC [Contains: 67 kDa matrix metalloproteinase-9
      • 82 kDa matrix metalloproteinase-9].
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P14780 # May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly- -Leu bond.
      COFACTOR: Binds 2 zinc ions per subunit. & Binds 3 calcium ions per subunit.
      SIZE: 707 amino acids; 78427 Da
      SUBUNIT: Exists as monomer, disulfide-linked homodimer, and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form.
      TISSUE SPECIFICITY: Produced by normal alveolar macrophages and granulocytes.
      DOMAIN: SwissProt: P14780 The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
      PTM: Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
      SIMILARITY: Belongs to the peptidase M10A family. & Contains 3 fibronectin type-II domains. & Contains 4 hemopexin-like domains.
      MISCELLANEOUS: In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Availability by Geography
      • This product is not available for sale in Japan.
      Usage Statement
      • Manufactured by Daiichi Fine Chemical Co., Ltd
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain at 2-8°C in undiluted aliquots for up to 12 months from date of receipt.

      During shipment, small volumes of product will occasionally become entrapped in the seal of the product vial. For products with volumes of 200μL or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container's cap.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information


      Anti-MMP-9 Antibody, clone GE-213 SDS


      Safety Data Sheet (SDS) 

      Anti-MMP-9 Antibody, clone GE-213 Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-HUMAN MMP-9 - 3263280 3263280
      MOUSE ANTI-HUMAN MMP-9 - 3458090 3458090
      MOUSE ANTI-HUMAN MMP-9 - 3607141 3607141
      MOUSE ANTI-HUMAN MMP-9 -2739387 2739387
      MOUSE ANTI-HUMAN MMP-9 -2776851 2776851
      MOUSE ANTI-HUMAN MMP-9 -2792497 2792497


      Reference overviewPub Med ID
      HPV16 oncoproteins induce MMPs/RECK-TIMP-2 imbalance in primary keratinocytes: possible implications in cervical carcinogenesis.
      Cardeal, LB; Boccardo, E; Termini, L; Rabachini, T; Andreoli, MA; di Loreto, C; Longatto Filho, A; Villa, LL; Maria-Engler, SS
      PloS one  7  e33585  2012

      Show Abstract
      22438955 22438955
      Tumor-associated macrophages provide a suitable microenvironment for non-small lung cancer invasion and progression.
      Rui Wang,Jie Zhang,Sufeng Chen,Meng Lu,Xiaoyang Luo,Shihua Yao,Shilei Liu,Ying Qin,Haiquan Chen
      Lung cancer (Amsterdam, Netherlands)  74  2011

      Show Abstract
      21601305 21601305
      Matrix metalloproteinase-9 is upregulated in nucleophosmin-anaplastic lymphoma kinase-positive anaplastic lymphomas and activated at the cell surface by the chaperone heat shock protein 90 to promote cell invasion.
      Lagarrigue, F; Dupuis-Coronas, S; Ramel, D; Delsol, G; Tronchère, H; Payrastre, B; Gaits-Iacovoni, F
      Cancer research  70  6978-87  2010

      Show Abstract
      20699364 20699364
      Mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis.
      Kyriakides, TR; Wulsin, D; Skokos, EA; Fleckman, P; Pirrone, A; Shipley, JM; Senior, RM; Bornstein, P
      Matrix biology : journal of the International Society for Matrix Biology  28  65-73  2009

      Show Abstract
      19379668 19379668
      Macrophage fusion, giant cell formation, and the foreign body response require matrix metalloproteinase 9.
      MacLauchlan, S; Skokos, EA; Meznarich, N; Zhu, DH; Raoof, S; Shipley, JM; Senior, RM; Bornstein, P; Kyriakides, TR
      Journal of leukocyte biology  85  617-26  2009

      Show Abstract
      19141565 19141565
      Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species.
      Roy, R; Louis, G; Loughlin, KR; Wiederschain, D; Kilroy, SM; Lamb, CC; Zurakowski, D; Moses, MA
      Clinical cancer research : an official journal of the American Association for Cancer Research  14  6610-7  2008

      Show Abstract
      18927302 18927302
      Reduced expression of inducible gelatinase B/matrix metalloproteinase-9 in monocytes from patients with myelodysplastic syndrome: Correlation of inducible levels with the percentage of cytogenetically marked cells and with marrow cellularity.
      Mineo Iwata,Manoj Pillai,Aravind Ramakrishnan,Robert C Hackman,H Joachim Deeg,Ghislain Opdenakker,Beverly Torok-Storb,H Joachim Deeg
      Blood  109  2007

      Show Abstract Full Text Article
      16954500 16954500
      Increased tissue factor, MMP-8, and D-dimer expression in diabetic patients with unstable advanced carotid atherosclerosis.
      Krupinski, J; Turu, MM; Font, MA; Ahmed, N; Sullivan, M; Rubio, F; Badimon, L; Slevin, M
      Vascular health and risk management  3  405-12  2007

      Show Abstract
      17969370 17969370
      Intraplaque MMP-8 levels are increased in asymptomatic patients with carotid plaque progression on ultrasound.
      Marta Miguel Turu, Jerzy Krupinski, Esther Catena, Ana Rosell, Joan Montaner, Francisco Rubio, Jose Alvarez-Sabin, Marc Cairols, Lina Badimon
      Atherosclerosis  187  161-9  2006

      Show Abstract
      16259988 16259988
      Matrix metalloproteinase expression in basal cell carcinoma: relationship between enzyme profile and collagen fragmentation pattern.
      Taskin Yucel, Amar Mutnal, Kevin Fay, Suzanne E G Fligiel, Timothy Wang, Timothy Johnson, Shan R Baker, James Varani
      Experimental and molecular pathology  79  151-60  2005

      Show Abstract
      16004981 16004981

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      Life Science Research > Antibodies and Assays > Primary Antibodies