Recombinant Human MMP-8 Protein, CF
Recombinant Human MMP-8 Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Supplied as a 0.2 μm filtered solution in Tris, NaCl and CaCl2.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5 (TCNB)
- Recombinant Human MMP‑8 (rhMMP-8) (Catalog # 908-MP)
- p-aminophenylmercuric acetate (APMA) (Sigma, Catalog # A-9563), 100 mM stock in DMSO
- Substrate: MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (Catalog # ES001), 2 mM stock in DMSO
- F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
- Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
- Activate rhMMP-8 at 100 µg/mL with 1 mM APMA in Assay Buffer.
- Incubate reaction at 37 °C for 1 hour.
- Dilute activated rhMMP-8 to 1.0 ng/µL in Assay Buffer.
- Dilute Substrate to 20 µM in Assay Buffer.
- In a plate load 50 µL of 1.0 ng/µL rhMMP-8, and start the reaction by adding 50 µL of 20 µM Substrate to wells. 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).Per Well:
- rhMMP-8: 0.050 µg
- Substrate: 10 µM
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the 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. MMP-8 is heavily glycosylated.
Citations for Recombinant Human MMP-8 Protein, CF
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.
Citations: Showing 1 - 6
Filter your results:
Breast cancer cells rely on environmental pyruvate to shape the metastatic niche
Authors: I Elia, M Rossi, S Stegen, D Broekaert, G Doglioni, M van Gorsel, R Boon, C Escalona-N, S Torrekens, C Verfaillie, E Verbeken, G Carmeliet, SM Fendt
Sample Types: Spheroids
Matrix Metalloproteinase Triple-Helical Peptide Inhibitors: Potential Cross-Reactivity with Caspase-11
Authors: AM Knapinska, M Hart, G Drotleff, GB Fields
Sample Types: Peptide
Lytic and mechanical stability of clots composed of fibrin and blood vessel wall components.
Authors: Rottenberger Z, Komorowicz E, Szabo L, Bota A, Varga Z, Machovich R, Longstaff C, Kolev K
J Thromb Haemost, 2013;11(3):529-38.
Sample Types: Recombinant Protein
Applications: Enzyme Assay
Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.
Authors: Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura E, Dive V
J Biol Chem, 2012;287(32):26647-56.
Sample Types: Fluorogenic Peptide Substrate
Applications: Enzyme Assay
Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp).
Authors: Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y
J. Bone Miner. Res., 2010;26(0):220.
Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients.
Authors: Gaggar A, Li Y, Weathington N, Winkler M, Kong M, Jackson P, Blalock JE, Clancy JP
Am. J. Physiol. Lung Cell Mol. Physiol., 2007;293(1):L96-L104.
Sample Types: N/A
Applications: Western Blot
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Fluorogenic Peptide Substrates
Reviews for Recombinant Human MMP-8 Protein, CF
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