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Human/Primate MMP-7 Antibody

Catalog #: MAB9072
2 Citations Datasheet
Catalog # Availability Size / Price Qty
MAB9072-SP
MAB9072-500
MAB9072-100
Product Details
Citations (2)
FAQs
Supplemental Products
Reviews
Summary Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Human/Primate MMP-7 Antibody Summary

Species Reactivity
Human, Primate
Specificity
Detects human and primate MMP-7 in ELISAs. In sandwich immunoassays, no cross-reactivity or interference with recombinant human (rh) MMP-1, 2, 3, 8, 9, 10, 13, recombinant mouse MMP-7, 9, rhTIMP-1, 2, 3, or 4 is observed.
Source
Monoclonal Mouse IgG1 Clone # 111439
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Mouse myeloma cell line NS0-derived recombinant human MMP‑7
Leu18-Lys267 (Ala230del)
Accession # NP_002414
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample

Human/Primate MMP-7 Sandwich Immunoassay

Recommended Concentration
Reagent
ELISA Capture (Matched Antibody Pair)
2-8 µg/mL 

Use in combination with:

Detection Reagent: Human/Primate MMP‑7 Biotinylated Antibody (Catalog # BAF907)

Standard: Recombinant Human MMP-7 Protein, CF (Catalog # 907-MP)

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.

Preparation and Storage

Reconstitution
Reconstitute at 0.5 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
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

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Citations for Human/Primate MMP-7 Antibody

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.

2 Citations: Showing 1 - 2
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  1. Pilot Application of Magnetic Nanoparticle-Based Biosensor for Necrotizing Enterocolitis
    Authors: Dokyoon Kim, Changlin Fu, Xuefeng B Ling, Zhongkai Hu, Guozhong Tao, Yingzhen Zhao et al.
    Journal of Proteomics & Bioinformatics
  2. Synergism between Hedgehog-GLI and EGFR Signaling in Hedgehog-Responsive Human Medulloblastoma Cells Induces Downregulation of Canonical Hedgehog-Target Genes and Stabilized Expression of GLI1
    Authors: Frank Götschel, Daniela Berg, Wolfgang Gruber, Christian Bender, Markus Eberl, Myriam Friedel et al.
    PLoS ONE

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