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.
Monoclonal Mouse IgG2B Clone # 111433
Protein A or G purified from ascites
Mouse myeloma cell line NS0-derived recombinant human MMP‑7 Leu18-Lys267 (Ala230del) Accession # NP_002414.1
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.
Immersion fixed paraffin-embedded sections of human pancreatic cancer tissue
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
Reconstitute at 0.5 mg/mL in sterile PBS.
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.
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.
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