Recombinant Human MMP-8 Protein, CF

• Reactivity: Hu
• Applications: Enzyme Activity
• Format: Carrier-Free

Recombinant Human MMP-8 Protein, CF Summary

• Details of Functionality: Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH 2 (Catalog # ES001). The specific activity is >250 pmol/min/µg, as measured under the described conditions.
• Source: Mouse myeloma cell line, NS0-derived human MMP-8 protein Phe21-Gly467
• Accession #: AAZ38714
• N-terminal Sequence: Phe21
• Structure / Form: Pro form
• Protein/Peptide Type: Recombinant Enzymes
• Gene: MMP8
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Enzyme Activity
• Theoretical MW: 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.
• SDS-PAGE: 70 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  6 months from date of receipt, -70 degreesC as supplied. 3 months, -70 degreesC under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in Tris, NaCl and CaCl 2 .
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Assay Procedure:
  • 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
  1. Activate rhMMP-8 at 100 µg/mL with 1 mM APMA in Assay Buffer.
  2. Incubate reaction at 37 °C for 1 hour.
  3. Dilute activated rhMMP-8 to 1.0 ng/µL in Assay Buffer.
  4. Dilute Substrate to 20 µM in Assay Buffer.
  5. 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.
  6. Read at excitation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes.
  7. 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

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human MMP-8 Protein, CF

• CLG1HNC
• Collagenase 2
• EC 3.4.24
• EC 3.4.24.34
• matrix metallopeptidase 8 (neutrophil collagenase)
• matrix metalloproteinase 8 (neutrophil collagenase)
• Matrix metalloproteinase-8
• MMP8
• MMP-8
• neutrophil collagenase
• PMNL collagenase
• PMNL-CL

Background

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.

Publications for MMP-8 (908-MP)(12)

Publications using 908-MP

• Caton, ER;Pan, Y;Kiser, KM;Haddaway, CR;Bryden, WA;McLoughlin, M;Mirski, MA;Christenson, RH;Sevilla, CC;Feng, S;Chen, S;Chen, D; Rapid sepsis diagnosis with protease activity measurement medRxiv : the preprint server for health sciences 2025-07-15 [PMID: 40791693] (Bioassay, Human)
• Stocks, B;Quesada, JP;Mozzicato, AM;Jacob, C;Jensen, S;MacGregor, KA;Bangsbo, J;Zierath, JR;Hostrup, M;Deshmukh, AS; Temporal dynamics of the interstitial fluid proteome in human skeletal muscle following exhaustive exercise Science advances 2025-01-31 [PMID: 39889004] (Bioassay, Human)
• Y Ghochani, SD Muthukrish, A Sohrabi, R Kawaguchi, MC Condro, S Bastola, F Gao, Y Qin, J Mottahedeh, ML Iruela-Ari, N Rao, DR Laks, LM Liau, GW Mathern, SA Goldman, ST Carmichael, I Nakano, G Coppola, SK Seidlits, HI Kornblum A molecular interactome of the glioblastoma perivascular niche reveals integrin binding sialoprotein as a mediator of tumor cell migration Cell Reports, 2022-10-18;41(3):111511. 2022-10-18 [PMID: 36261010] (Bioassay, Human)
• QC Larrouture, AP Cribbs, SR Rao, M Philpott, SJ Snelling, HJ Knowles Loss of mutual protection between human osteoclasts and chondrocytes in damaged joints initiates osteoclast-mediated cartilage degradation by MMPs Scientific Reports, 2021-11-22;11(1):22708. 2021-11-22 [PMID: 34811438] (Zymography Control, Human)
• K Juurikka, A Dufour, K Pehkonen, B Mainoli, P Campioni R, N Solis, T Klein, P Nyberg, CM Overall, T Salo, P Åström MMP8 increases tongue carcinoma cell-cell adhesion and diminishes migration via cleavage of anti-adhesive FXYD5 Oncogenesis, 2021-05-31;10(5):44. 2021-05-31 [PMID: 34059618] (Bioassay, Human)
• J Cassuto, A Folestad, J Göthlin, H Malchau, J Kärrholm Concerted actions by MMPs, ADAMTS and serine proteases during remodeling of the cartilage callus into bone during osseointegration of hip implants Bone Rep, 2020-09-11;13(0):100715. 2020-09-11 [PMID: 32995386] (ELISA Detection, Human)
• AM Knapinska, M Hart, G Drotleff, GB Fields Matrix Metalloproteinase Triple-Helical Peptide Inhibitors: Potential Cross-Reactivity with Caspase-11 Molecules, 2019-11-28;24(23):. 2019-11-28 [PMID: 31795279] (Bioassay, Human)
• 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 Breast cancer cells rely on environmental pyruvate to shape the metastatic niche Nature, 2019-02-27;0(0):. 2019-02-27 [PMID: 30814728] (Bioassay, Human)
• Rottenberger Z, Komorowicz E, Szabo L, Bota A, Varga Z, Machovich R, Longstaff C, Kolev K Lytic and mechanical stability of clots composed of fibrin and blood vessel wall components. J Thromb Haemost, 2013-03-01;11(3):529-38. 2013-03-01 [PMID: 23279194] (Enzyme Assay, Human)
• Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura E, Dive V Simple pseudo-dipeptides with a P2&#039; glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins. J Biol Chem, 2012-06-11;287(32):26647-56. 2012-06-11 [PMID: 22689580] (Enzyme Assay)
• Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp). J. Bone Miner. Res., 2011-01-01;26(0):220. 2011-01-01 [PMID: 20687161] (Bioassay, Human)
• Gaggar A, Li Y, Weathington N, Winkler M, Kong M, Jackson P, Blalock JE, Clancy JP Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients. Am. J. Physiol. Lung Cell Mol. Physiol., 2007-03-23;293(1):L96-L104. 2007-03-23 [PMID: 17384080] (Bioassay, N/A)

Bioinformatics

• Gene Symbol: MMP8
• Uniprot:
  • AAZ38714()