Human MMP-9 Antibody

(13 citations)   
  • Species Reactivity
    Human
  • Specificity
    Detects human MMP-9 in Western blots. In Western blots, reactivity with the pro (92 kDa), active (82 kDa), and C-terminal truncated (65 kDa) forms of recombinant human (rh) MMP-9 is observed. Also in Western blots, 20% cross-reactivity with rhMMP-2, 5% cross‑reactivity with rhMMP-1, and no cross-reactivity with rhMMP-3, -7, -8, -10, -12, or -13 is observed.
  • Source
    Monoclonal Mouse IgG1 Clone # 4H3
  • Purification
    Protein A or G purified from ascites
  • Immunogen
    Chinese hamster ovary cell line CHO-derived recombinant human MMP-9
  • 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
    2 µg/mL
    See below
  • Immunohistochemistry
    25-100 µg/mL
    Immersion fixed paraffin-embedded sections of human ovarian and breast cancer tissues
  • Immunoprecipitation
    25 µg/mL
    Conditioned cell culture medium spiked with Recombinant Human MMP‑9 (Catalog # 911-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‑9 by Western Blot. Western blot shows lysates of U937 human histiocytic lymphoma cell line untreated (-) or treated (+) with 5 ng/mL PMA for 24 hours. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human MMP‑9 Monoclonal Antibody (Catalog # MAB911) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018).
A specific band was detected for MMP‑9 at approximately 85 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-9
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (Gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain.
  • Long Name:
    Matrix Metalloproteinase 9
  • Entrez Gene IDs:
    4318 (Human); 17395 (Mouse); 81687 (Rat)
  • Alternate Names:
    92 kDa gelatinase; 92 kDa type IV collagenase; CLG4B; EC 3.4.24; EC 3.4.24.35; Gelatinase B; GELB; macrophage gelatinase; MANDP2; matrix metallopeptidase 9; matrix metalloproteinase 9; matrix metalloproteinase-9; MMP9; MMP-9; type V collagenase
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.

13 Citations: Showing 1 - 10
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Species
Applications
Sample Type
  1. Diverse matrix metalloproteinase functions regulate cancer amoeboid migration.
    Authors: Orgaz J, Pandya P, Dalmeida R, Karagiannis P, Sanchez-Laorden B, Viros A, Albrengues J, Nestle F, Ridley A, Gaggioli C, Marais R, Karagiannis S, Sanz-Moreno V
    Nat Commun, 2014;5(0):4255.
    Species: Human
    Sample Type: Cell Lysates
    Application: WB
  2. High matrix metalloproteinase production correlates with immune activation and leukocyte migration in leprosy reactional lesions.
    Authors: Teles RM, Teles RB, Amadeu TP, Moura DF, Mendonca-Lima L, Ferreira H, Santos IM, Nery JA, Sarno EN, Sampaio EP
    Infect. Immun., 2010;78(3):1012-21.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC Frozen
  3. The DSCs-expressed CD82 controls the invasiveness of trophoblast cells via integrinbeta1/MAPK/MAPK3/1 signaling pathway in human first-trimester pregnancy.
    Authors: Li MQ, Hou XF, Shao J, Tang CL, Li DJ
    Biol. Reprod., 2010;82(5):968-79.
    Species: Human
    Sample Type: Whole Cells
    Application: Cell-based ELISA
  4. Mediators of glioblastoma resistance and invasion during antivascular endothelial growth factor therapy.
    Authors: Lucio-Eterovic AK, Piao Y, de Groot JF
    Clin. Cancer Res., 2009;15(14):4589-99.
    Species: Human
    Sample Type: Cell Culture Supernates
    Application: WB
  5. 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
  6. Long-term weight loss decreases the nontraditional cardiovascular risk factors interleukin-18 and matrix metalloproteinase-9 in obese subjects.
    Authors: Madsen EL, Bruun JM, Skogstrand K, Hougaard DM, Christiansen T, Richelsen B
    Metab. Clin. Exp., 2009;58(7):946-53.
    Species: Human
    Sample Type: Serum
    Application: Luminex Assay Development
  7. Expression pattern and circulating levels of endostatin in patients with pancreas cancer.
    Authors: Ohlund D, Ardnor B, Oman M, Naredi P, Sund M
    Int. J. Cancer, 2008;122(12):2805-10.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC Frozen
  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
  9. Neutrophil gelatinase-associated lipocalin is expressed in osteoarthritis and forms a complex with matrix metalloproteinase 9.
    Authors: Gupta K, Shukla M, Cowland JB, Malemud CJ, Haqqi TM
    Arthritis Rheum., 2007;56(10):3326-35.
    Species: Human
    Sample Type: Synovial Fluid
    Application: IP
  10. Hypoxia-induced mediators of stem/progenitor cell trafficking are increased in children with hemangioma.
    Authors: Kleinman ME, Greives MR, Churgin SS, Blechman KM, Chang EI, Ceradini DJ, Tepper OM, Gurtner GC
    Arterioscler. Thromb. Vasc. Biol., 2007;27(12):2664-70.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC Paraffin-embedded
  11. Role of platelet-derived growth factor and transforming growth factor beta1 the in the regulation of metalloproteinase expressions.
    Authors: Borrelli V, di Marzo L, Sapienza P, Colasanti M, Moroni E, Cavallaro A
    Surgery, 2006;140(3):454-63.
    Species: Human
    Sample Type: Cell Culture Supernates
    Application: WB
  12. Control of matrix metalloproteinase production in human intestinal fibroblasts by interleukin 21.
    Authors: Monteleone G, Caruso R, Fina D, Peluso I, Gioia V, Stolfi C, Fantini MC, Caprioli F, Tersigni R, Alessandroni L, MacDonald TT, Pallone F
    Gut, 2006;55(12):1774-80.
    Species: Human
    Sample Type: Cell Lysates
    Application: WB
  13. Neutrophil-derived metalloproteinase-9 predicts healing quality after sinus surgery.
    Authors: Watelet JB, Demetter P, Claeys C, Van Cauwenberge P, Cuvelier C, Bachert C
    Laryngoscope, 2005;115(1):56-61.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC Paraffin-embedded
Expand to show all 13 Citations
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