• Species Reactivity

  Mouse

• Specificity

  Detects the pro form of mouse MMP-7 in direct ELISAs and Western blots. In Western blots, no cross-reactivity with recombinant mouse MMP‑2, -3, -8, -9, -12, or -24 is observed.

• Source

  Monoclonal Rat IgG    _2B Clone # 377313

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant mouse MMP‑7    
  Leu18-Leu264    
  Accession # AAA99983

• 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

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

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 (1). 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.

• References:

1. Woessner, J.F. (2004) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al. eds. p. 532.

• 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