>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
71 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-2 to 100 µg/mL in Assay Buffer.
Activate rhMMP-2 by adding APMA to a final concentration of 1 mM.
Incubate at 37 °C for 1 hour.
Dilute activated rhMMP-2 to 0.2 ng/µL in Assay Buffer.
Dilute Substrate to 20 µM in Assay Buffer.
Load into a black well plate 50 µL of the 0.2 ng/µL rhMMP-2 and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 20 µM Substrate.
Read at excitation 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-2: 0.010 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-2 Protein, CF
72 kDa gelatinase
CLG4A72 kDa type IV collagenase
collagenase type IV-A
matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase)
matrix metalloproteinase 2 (gelatinase A, 72kD gelatinase, 72kD type IVcollagenase)
TBE-1matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase)
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-2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP-2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites.
MMP-2: More Than a Cancer Marker Matrix metalloproteinases (MMP) are a family of endopeptidases involved in the breakdown of extracellular matrix (ECM) during both normal physiological and disease processes. MMP-2 is a zinc-dependent family member that selectively cleaves collagen... Read full blog post.
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