>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
52 kDa and 51 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.
p-aminophenylmercuric acetate (APMA) (Sigma, Catalog # A-9563), 100 mM stock in DMSO
Substrate MCA-Lys-Pro-Leu-Gly-Leu-DAP(DNP)-Ala-Arg-NH2 (Catalog # ES010), 2 mM stock in DMSO
F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rmMMP-8 to 20 µg/mL in Assay Buffer.
Activate rmMMP-8 by adding APMA to a final concentration of 1 mM.
Incubate at room temperature for 2 hours.
Dilute activated rmMMP-8 to 0.5 ng/µL in Assay Buffer.
Dilute Substrate to 80 µM in Assay Buffer.
Load into a black well plate 50 µL of 0.5 ng/µL rmMMP-8, and start the reaction by adding 50 µL of 80 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 80 µM Substrate without any rmMMP-8.
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).
rmMMP-8: 0.025 μg
Substrate: 40 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse MMP-8 Protein, CF
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade many components of the extracellular matrix. MMP-8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP-8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-alpha and GM-CSF. MMP-8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta -casein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis, MMP‑8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP-8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexin-like domain.
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