Human/Primate MMP-3 Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF513
Product Details
Citations (2)
FAQs
Supplemental Products
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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.

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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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