Recombinant Human MMP-8 Protein, CF

Images

 
There are currently no images for MMP-8 (908-MP).

Every product we sell is backed by Novus' 100% Guarantee. If you have used this product, please submit your images and reviews to earn reward points.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human MMP-8 Protein, CF Summary

Details of Functionality
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (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 #
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
Publications
Read Publications using
908-MP in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl and CaCl2.
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.

Customers Who Viewed This Item Also Viewed...

DMP900
Species: Hu
Applications: ELISA
MMP200
Species: Ca, Hu, Mu, Po, Rt
Applications: ELISA
DTM100
Species: Hu
Applications: ELISA
DM1300
Species: Hu
Applications: ELISA
DMP100
Species: Hu
Applications: ELISA
DMP300
Species: Hu
Applications: ELISA
H00006936-B01P
Species: Hu
Applications: ICC/IF, WB
DTM200
Species: Hu
Applications: ELISA
DMP700
Species: Hu
Applications: ELISA
NBP2-67415
Species: Hu, Mu, Rt
Applications: Flow, ICC/IF, IHC, IHC-P, IP, WB
D6050
Species: Hu
Applications: ELISA
MAB9167
Species: Hu
Applications: CyTOF-ready, Flow, ICC, IHC, WB
MAB208
Species: Hu
Applications: CyTOF-ready, ELISA(Cap), ELISA(Det), ELISA(Sta), ICC, ICFlow, Neut, Simple Western, WB

Publications for MMP-8 (908-MP)(9)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 5 applications: Bioassay, ELISA Detection, Enzyme Assay, Western Blot, Zymography Control.


Filter By Application
Bioassay
(4)
ELISA Detection
(1)
Enzyme Assay
(2)
Western Blot
(1)
Zymography Control
(1)
All Applications
Filter By Species
Human
(7)
N/A
(2)
All Species
Showing Publications 1 - 9 of 9.
Publications using 908-MP Applications Species
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(1):22708. 2021 [PMID: 34811438] (Zymography Control, Human) 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;10(5):44. 2021 [PMID: 34059618] (Bioassay, Human) 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;13(0):100715. 2020 [PMID: 32995386] (ELISA Detection, Human) 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;24(23):. 2019 [PMID: 31795279] (Bioassay, Human) 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;0(0):. 2019 [PMID: 30814728] (Bioassay, Human) 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;11(3):529-38. 2013 [PMID: 23279194] (Enzyme Assay, Human) 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;287(32):26647-56. 2012 [PMID: 22689580] (Enzyme Assay, N/A) Enzyme Assay N/A
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., 2010;26(0):220. 2010 [PMID: 20687161] (Bioassay, Human) 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;293(1):L96-L104. 2007 [PMID: 17384080] (Western Blot, N/A) Western Blot N/A

Reviews for MMP-8 (908-MP) (0)

There are no reviews for MMP-8 (908-MP). By submitting a review you will receive an Amazon e-Gift Card or Novus Product Discount.
  • Review with no image -- $10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen
  • Review with an image -- $25/€18/£15/$25 CAD/¥150 Yuan/¥2500 Yen

FAQs for MMP-8 (908-MP) (0)

There are no specific FAQs related to this product. Read our general customer & technical service FAQs.

Customers Who Bought This Also Bought

Contact Information

Product PDFs

Calculators

Concentration Calculator

The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.

=
÷

Review this Product

Be the first to review our Recombinant Human MMP-8 Protein, CF and receive a gift card or discount.

Bioinformatics

Gene Symbol MMP8
Uniprot