Recombinant Human MMP-13 Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 511-MM
Key Product Details
Source
NS0
Accession #
Structure / Form
Pro form
Conjugate
Unconjugated
Applications
Enzyme Activity
Product Specifications
Source
Mouse myeloma cell line, NS0-derived human MMP-13 protein
Leu20-Cys471
Leu20-Cys471
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
Leu20
Predicted Molecular Mass
52 kDa
SDS-PAGE
58 kDa, reducing conditions
Activity
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001).
The specific activity is >2,000 pmol/min/µg, as measured under the described conditions.
The specific activity is >2,000 pmol/min/µg, as measured under the described conditions.
Reviewed Applications
Read 2 reviews rated 5 using 511-MM in the following applications:
Formulation, Preparation and Storage
511-MM
| Formulation | Supplied as a 0.2 μm filtered solution in MES, NaCl, CaCl2 and Brij-35. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: MMP-13
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-13 (Collagenase-3) has been demonstrated to degrade a range of extracellular matrix proteins, including collagen types I, II, III, IV, IX, X and XIV, gelatin, aggrecan, perlecan and fibronectin. MMP-13 is distinguished from the other human collagenases by its effecient degradation of type II collagen. MMP-13 is expressed by fibroblasts, chrondrocytes and squamous epithelial cells. Structurally, MMP-13 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.
References
- Jeffery, J.J. (1998) in Collagenase 3. A.J. Barrett, et al. (eds): Handbook of Proteolytic Enzymes, San Diego: Academic Press, p. 1167.
Long Name
Matrix Metalloproteinase 13
Alternate Names
MMP13
Entrez Gene IDs
4322 (Human)
Gene Symbol
MMP13
UniProt
Additional MMP-13 Products
Product Documents for Recombinant Human MMP-13 Protein, CF
Product Specific Notices for Recombinant Human MMP-13 Protein, CF
For research use only
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