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Human/Primate MMP-7 Biotinylated Antibody

Catalog #: BAF907
2 Citations Datasheet
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BAF907
Product Details
Citations (2)
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Summary Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Human/Primate MMP-7 Biotinylated Antibody Summary

Species Reactivity
Human, Primate
Specificity
Detects human and primate MMP-7 in ELISAs and Western blots. In sandwich immunoassays, less than 0.1% cross-reactivity with recombinant human (rh) MMP‑1, rhMMP-2, rhMMP-3, rhMMP-4, rhMMP-8, rhMMP-9, rhMMP-10, rhMMP-13, recombinant mouse (rm) MMP-7, rmMMP-9, and
rhTIMP-1, rhTIMP--2, rhTIMP-3, and rhTIMP-4 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human MMP‑7
Leu18-Lys267
Accession # P09237
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human MMP‑7 (Catalog # 907-MP)

Human/Primate MMP-7 Sandwich Immunoassay

Recommended Concentration
Reagent
ELISA Detection (Matched Antibody Pair)
0.1-0.4 µg/mL 

Use in combination with:

Capture Reagent: Human/Primate MMP‑7 Antibody (Catalog # MAB9072)

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 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it 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 Biotinylated 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. 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
  2. Urinary matrix metalloproteinase-7 level is associated with the presence of metastasis in bladder cancer.
    Authors: Szarvas T, Singer BB, Becker M, vom Dorp F, Jager T, Szendroi A, Riesz P, Romics I, Rubben H, Ergun S
    BJU Int., 2010-09-03;107(7):1069-73.
    Species: Human
    Sample Types: Urine
    Applications: Western Blot

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