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CC1048 MMP-9, human, proform

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CC1048
5 µg  
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      Tableau de caractéristiques principal

      Key ApplicationsEntrez Gene NumberSpeciesUni Prot Number
      FUNCNM_004994.2 Human P14780
      Description
      Catalogue NumberCC1048
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionMMP-9, human, proform
      OverviewCC1048 is isolated from human blood. The preparation is free from MMP-9 dimer and from complexes of MMP-9 with TIMP-1 or lipocalin. Upon activation with trypsin, enzymatically active MMP-9 of Mr 86 kDa is formed.

      INHIBITORS:

      MMP-9 is inhibited by TIMPs and by chelators of divalent cations, such as EDTA or o-phenanthroline.
      Alternate Names
      • Progelatinase B
      • 92 kDa Type IV Collagenase
      Background InformationHuman MMP-9 consists of 668 amino acids with a calculated Mrof 76 240 Da. Due to N- and O-linked glycosylated the Mr in SDS-PAGE is about 92 kDa [Wilhelm et al., 1989]. Within the protein sequence, the following structural domains can be distinguished [Wilhelm et al., 1989; Collier, et al., 1991]: An N-terminal propeptide, which confers latency to the proenzyme, a Ca2+ and Zn2+ ion-binding catalytic domain containing an insertion of three repeats homologous to type II repeats in the gelatin-binding region of fibronectin, and a C-terminal hemopexin-like domain. Catalytic and hemopexin domains are connected by a proline-rich sequence with homology to sequences in collagens. The gelatin-binding region and the hemopexin domain confer specific macromolecular substrate binding to MMP-9. The hemopexin domain of the latent enzyme binds TIMP-1 [Wilhelm et al., 1989; Goldberg et al., 1992; Kolkenbrock et al., 1995].

      Activation of latent MMP-9 can be mediated by proteases like stromelysin, cathepsin G, kallikrein and trypsin or by incubation with APMA [Murphy & Grabbe, 1995]. In the presence of APMA, the propeptide is not removed completely, however, and there occurs considerable C-terminal self-processing [Murphy & Grabbe, 1995]. The enzyme is inhibited by TIMP-1 and TIMP-2.

      MMP-9 is secreted from macrophages, polymorphonuclear leukocytes, keratinocytes and many tumor cells [Hibbs et al., 1984; Sato et al., 1991; Sato et al., 1992]. It is detected in human plasma [Zucker et al., 1993] and saliva [Makela et al., 1994].

      MMP-9 is involved in physiological processes such as angiogenesis, wound healing, bone remodeling, migration of macrophages and leukocytes [Shapiro, 1998]. Hydrolysis of type IV collagen and other matrix proteins in basement membranes by MMP-9 contributes to tumor cell invasion [Bernhard et al., 1994] and aortic aneurysm formation [Thompson, 1995].
      Product Information
      PresentationProvided as a liquid in 50 mM Tris-HCl, pH 7.0, 200 mM NaCl, 5 mM CaCl2, ,1 μM ZnCl2, 0.05% Brij-35, 0.05% NaN3.
      Quality LevelMQ100
      Applications
      Key Applications
      • Affects Function
      Application NotesACTIVATION:

      An aliquot of 10 μL MMP-9 monomer is mixed with 20 μL trypsin solution (see below) and activation buffer in a total volume of 100 μL. The mixture is incubated for 20 min at 37°C. Thereafter trypsin is inhibited by addition of 10 μL aprotinin solution.

      Trypsin solution: 0.50 mg TPCK-trypsin/mL activation buffer. The solution is stored in aliquots at -20°C.

      Activation Buffer: 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl2.

      Aprotinin solution: 1 mg aprotinin/mL activation buffer. The solution is stored at -20°C.
      Biological Information
      Concentration5 mg/25 mL
      PurityMMP-9 monomer appears as a major band at 92 kDa in non-reducing SDS-PAGE (>95% of total protein).
      Specific ActivitySPECIFIC ACTIVITY: <br /><br />The specific activity of activated MMP-9 after trypsin activation is >1200 mU/mg, where 1 U is the activity that hydrolyzes 1 mmol peptide (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dpa-Ala-Arg) within 1 minute under the assay conditions described by Knight ,et al. When measured with the peptide substrate dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg [Masui et al., 1977] the specific activity of MMP-9 monomer is >1500 mU/mg.
      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 3.4.24.35 [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.
      Product Usage Statements
      Usage Statement
      • 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 frozen at -70°C in undiluted aliquots. The enzyme may be stored at -20°C for several without significant loss of activity. Repeated freezing and thawing should be avoided.
      Packaging Information
      Material Size5 µg
      Global Trade Item Number
      Référence GTIN
      CC1048 04053252741098