Human/Primate MMP-7 Antibody

Catalog # Availability Size / Price Qty
MAB9072-SP
MAB9072-500
MAB9072-100
Product Details
Citations (2)
FAQs
Supplemental Products
Reviews

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.

Reconstitution Calculator

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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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