Human MMP-7 Antibody

(8 citations)   
  • Species Reactivity
    Human
  • Specificity
    Detects the pro and active forms of human MMP-7 in Western blots. In dot blots, approximately 20% cross-reactivity with recombinant human MMP-8 is observed and no cross-reactivity with recombinant human MMP-1, -2, -3, -9, -10, -12, or -13 is observed.
  • Source
    Monoclonal Mouse IgG2B Clone # 111433
  • Purification
    Protein A or G purified from ascites
  • Immunogen
    Mouse myeloma cell line NS0-derived recombinant human MMP‑7
    Leu18-Lys267 (Ala230del)
    Accession # NP_002414.1
  • Formulation
    Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
  • Label
    Unconjugated
Applications
  •  
    Recommended
    Concentration
    Sample
  • Western Blot
    1 µg/mL
    See below
  • Immunohistochemistry
    8-25 µg/mL
    Immersion fixed paraffin-embedded sections of human pancreatic cancer tissue
  • Immunoprecipitation
    25 µg/mL
    Conditioned cell culture medium spiked with Recombinant Human MMP‑7 (Catalog # 907-MP), see our available Western blot detection antibodies
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Data Examples
Detection of Human MMP‑7 by Western Blot. Western blot shows lysates of Capan‑1 human pancreatic adenocarcinoma cell line and SK‑OV‑3 human ovarian adenocarcinoma cell line and, for additional reference, Recombinant Human MMP-7 Western Blot Standard Protein (Catalog # WBC016). PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human MMP‑7 Monoclonal Antibody (Catalog # MAB9071) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for MMP‑7 at approximately 28 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
  • Reconstitution
    Reconstitute at 0.5 mg/mL in sterile PBS.
  • Shipping
    The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
  • Stability & Storage
    Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
    • 12 months from date of receipt, -20 to -70 °C as supplied.
    • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
    • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: MMP-7

Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin and versican. MMP-7 is implicated in the activation of other proteinases such as plasminogen, MMP-1, MMP-2, and MMP-9. In addition to its roles in connective tissue remodeling and cancer, MMP-7 also regulates intestinal alpha ‑defensin activation in innate host defense, releases tumor necrosis factor-alpha in a model of herniated disc resorption, and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site.

  • Long Name:
    Matrix Metalloproteinase 7
  • Entrez Gene IDs:
    4316 (Human); 17393 (Mouse)
  • Alternate Names:
    EC 3.4.24; EC 3.4.24.23; Matrilysin; matrin; matrix metallopeptidase 7 (matrilysin, uterine); matrix metalloproteinase 7 (matrilysin, uterine); Matrix metalloproteinase-7; MMP7; MMP-7; MPSL1; Pump-1 protease; PUMP1; PUMP-1; uterine matrilysin; Uterine metalloproteinase
Related Research Areas
Citations:

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

8 Citations: Showing 1 - 8
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Species
Applications
Sample Type
  1. Urinary matrix metalloproteinase-7 level is associated with the presence of metastasis in bladder cancer.
    Authors: Szarvas T, Singer BB, Becker M, vom Dorp F, Jager T, Szendroi A, Riesz P, Romics I, Rubben H, Ergun S
    BJU Int., 2011;107(7):1069-73.
    Species: Human
    Sample Type: Urine
    Application: IP
  2. Integrin alpha5beta1 facilitates cancer cell invasion through enhanced contractile forces.
    Authors: Mierke CT, Frey B, Fellner M, Herrmann M, Fabry B
    J. Cell. Sci., 2011;124(0):369-83.
    Species: Human
    Sample Type: Whole Cells
    Application: Flow
  3. Matrix metalloproteinase-7 as a marker of metastasis and predictor of poor survival in bladder cancer.
    Authors: Szarvas T, Becker M, vom Dorp F, Gethmann C, Totsch M, Bankfalvi A, Schmid KW, Romics I, Rubben H, Ergun S
    Cancer Sci., 2010;101(5):1300-8.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC Paraffin-embedded
  4. Matrix metalloproteinase activity in pediatric acute lung injury.
    Authors: Kong MY, Gaggar A, Li Y
    Int J Med Sci, 2009;6(1):9-17.
    Species: Human
    Sample Type: Tissue Secretion
    Application: WB
  5. Stable isotope dilution multidimensional liquid chromatography-tandem mass spectrometry for pancreatic cancer serum biomarker discovery.
    Authors: Yu KH, Barry CG, Austin D
    J. Proteome Res., 2009;8(3):1565-76.
    Species: Human
    Sample Type: Serum
    Application: WB
  6. Gingival fibroblast inhibits MMP-7: evaluation in an ex vivo aorta model.
    Authors: Gogly B, Fournier B, Couty L, Naveau A, Brasselet C, Durand E, Coulomb B, Lafont A
    J. Mol. Cell. Cardiol., 2009;47(2):296-303.
    Species: Rabbit
    Sample Type: Cell Culture Supernates
    Application: WB
  7. Divergent functions for airway epithelial matrix metalloproteinase 7 and retinoic acid in experimental asthma.
    Authors: Goswami S, Angkasekwinai P, Shan M, Greenlee KJ, Barranco WT, Polikepahad S, Seryshev A, Song LZ, Redding D, Singh B, Sur S, Woodruff P, Dong C, Corry DB, Kheradmand F
    Nat. Immunol., 2009;10(5):496-503.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC
  8. IL-21 is highly produced in Helicobacter pylori-infected gastric mucosa and promotes gelatinases synthesis.
    Authors: Caruso R, Fina D, Peluso I, Fantini MC, Tosti C, Del Vecchio Blanco G, Paoluzi OA, Caprioli F, Andrei F, Stolfi C, Romano M, Ricci V, MacDonald TT, Pallone F, Monteleone G
    J. Immunol., 2007;178(9):5957-65.
    Species: Human
    Sample Type: Cell Culture Supernates
    Application: WB
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