>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
52 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rhMMP-1 to 50 µg/mL in Assay Buffer.
Activate 50 µg/mL rhMMP-1 by adding APMA to a final concentration of 1 mM.
Incubate at 37 °C for 2 hours.
Dilute activated rhMMP-1 to 1 ng/µL in Assay Buffer.
Dilute Substrate to 20 µM in Assay Buffer.
Load into a black well plate 50 µL of 1 ng/µL rhMMP-1 and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer, 50 µL Substrate, and no rhMMP-1.
Read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes.
Calculate specific activity:
Specific Activity (pmol/min/µg) =
Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)
*Adjusted for Substrate Blank
**Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).
rhMMP-1: 0.050 µg
Substrate: 10 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human MMP-1 Protein, CF
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-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, alpha ‑1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL-1 beta, IGF-BP3, IGF-BP5, pro MMP-2 and pro MMP-9. A significant role of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into ¾, ¼ fragments. However, as the list of substrates above illustrates, the role of MMP-1 is more diverse than originally envisaged, and may involve enzyme cascades, cytokine regulation and cell surface molecule modulation. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 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.
Cawston, T.E. (2004) in Interstitial Collagenase. Barrett, A.J. et al. (eds): Handbook of Proteolytic Enzymes, San Diego: Academic Press, p. 472.
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