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Human/Primate MMP-3 Biotinylated Antibody

Catalog #: BAF513
2 Citations Datasheet
Catalog # Availability Size / Price Qty
BAF513
Product Details
Citations (2)
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Summary Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Human/Primate MMP-3 Biotinylated Antibody Summary

Species Reactivity
Human, Primate
Specificity
Detects human and primate MMP-3 in ELISAS  and Western blots. In sandwich immunoassays, less than 2.5% cross-reactivity with recombinant human (rh) MMP‑10 is observed and less than 0.1% cross-reactivity with rhMMP-1, -2, -7, -8, -9, -12, and -13 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human MMP‑3
Tyr18-Cys477 with a Lys45Glu substitution
Accession # P08254
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‑3 (Catalog # 513-MP)

Human/Primate MMP-3 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‑3 Antibody (Catalog # AF513)

Standard: Recombinant Human MMP-3 Protein, CF (Catalog # 513-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-3

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP‑3 (stromelysin-1), can degrade a broad range of substrates including collagen alpha  chains, aggrecan, laminin, fibronectin, elastin, casein, alpha -1 antitrypsin, myelin basic protein, IL-1 beta, IGFBP-3, pro-MMP-1, pro-MMP-7, pro-MMP-8, pro-MMP-9 and pro-MMP-13. MMP-3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP-3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP-3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP-3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP-3 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.

Long Name
Matrix Metalloproteinase 3
Entrez Gene IDs
4314 (Human); 17392 (Mouse)
Alternate Names
CHDS6; EC 3.4.24; EC 3.4.24.17; matrix metallopeptidase 3 (stromelysin 1, progelatinase); matrix metalloproteinase 3 (stromelysin 1, progelatinase); Matrix metalloproteinase-3; MGC126102; MGC126103; MMP3; MMP-3; proteoglycanase; SL-1; STMY; STMY1MGC126104; STR1; Stromelysin 1; stromelysin-1; transin-1

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Citations for Human/Primate MMP-3 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. Relevance of Plasma Matrix Metalloproteinase-9 for Bronchiolitis Obliterans Syndrome after Allogeneic Hematopoietic Cell Transplantation
    Authors: Yoshihiro Inamoto, Paul J. Martin, Lynn E. Onstad, Guang-Shing Cheng, Kirsten M. Williams, Iskra Pusic et al.
    Transplantation and Cellular Therapy
  2. Mapping Proteolytic Processing in the Secretome of Gastric Cancer-Associated Myofibroblasts Reveals Activation of MMP-1, MMP-2, and MMP-3
    Authors: Christopher Holmberg, Bart Ghesquière, Francis Impens, Kris Gevaert, J. Dinesh Kumar, Nicole Cash et al.
    Journal of Proteome Research

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