Recombinant Human MMP-13 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human MMP-13 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 >2,000 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human MMP-13 protein
Leu20-Cys471
Accession #
N-terminal Sequence
Leu20
Structure / Form
Pro form
Protein/Peptide Type
Recombinant Enzymes
Gene
MMP13
Purity
>95%, 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

Theoretical MW
52 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
58 kDa, reducing conditions
Publications
Read Publications using
511-MM 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, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl, CaCl2 and Brij-35.
Purity
>95%, 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% Brij-35 (w/v), pH 7.5 (TCNB)
  • Recombinant Human MMP-13 (rhMMP-13) (Catalog # 511-MM)
  • p-Aminophenylmercuric acetate (APMA), (Sigma, Catalog # A-9563) 100 mM stock in DMSO
  • Fluorogenic Peptide Substrate I: MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Catalog # ES001)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhMMP-13 to 100 µg/mL in Assay Buffer.
  2. Add APMA to a final concentration of 1 mM.
  3. Incubate at 37 °C for 2 hours to activate.
  4. Dilute activated rhMMP-13 to 0.2 ng/µL in Assay Buffer.
  5. Dilute Substrate to 20 µM in Assay Buffer.
  6. Load 50 µL of the 0.2 ng/µL rhMMP-13 into a black well plate 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.
  7. Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in kinetic mode for 5 minutes.
  8. 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-13: 0.010 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-13 Protein, CF

  • CLG 3
  • CLG3EC 3.4.24
  • collagenase 3
  • EC 3.4.24.-
  • EC 3.4.24.22
  • EC 3.4.24.24
  • EC 3.4.24.35
  • EC 3.4.24.65
  • EC 3.4.24.7
  • MANDP1
  • matrix metallopeptidase 13 (collagenase 3)
  • matrix metalloproteinase 13 (collagenase 3)
  • Matrix metalloproteinase-13
  • MMP13
  • MMP-13

Background

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-13 (Collagenase-3) has been demonstrated to degrade a range of extracellular matrix proteins, including collagen types I, II, III, IV, IX, X and XIV, gelatin, aggrecan, perlecan and fibronectin. MMP-13 is distinguished from the other human collagenases by its effecient degradation of type II collagen. MMP-13 is expressed by fibroblasts, chrondrocytes and squamous epithelial cells. Structurally, MMP-13 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.

  1. Jeffery, J.J. (1998) in Collagenase 3. A.J. Barrett, et al. (eds): Handbook of Proteolytic Enzymes, San Diego: Academic Press, p. 1167.

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511-MM
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Applications: Enzyme Activity

Publications for MMP-13 (511-MM)(5)

We have publications tested in 3 confirmed species: Human, Bovine, N/A.

We have publications tested in 5 applications: Bioassay, ELISA Standard, EnzAct, Enzyme Assay, WB Standard.


Filter By Application
Bioassay
(1)
ELISA Standard
(1)
EnzAct
(1)
Enzyme Assay
(1)
WB Standard
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Filter By Species
Human
(1)
Bovine
(1)
N/A
(3)
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Showing Publications 1 - 5 of 5.
Publications using 511-MM Applications Species
He Y, Zheng Q, Jiang M, Sun S, Christiansen T, Kassem M, Karsdal M, Bay-Jensen A The effect of protease inhibitors on the induction of osteoarthritis-related biomarkers in bovine full-depth cartilage explants. PLoS ONE, 2015;10(0):. 2015 [PMID: 25909781] (WB Standard, N/A) WB Standard N/A
Ozeki N, Kawai R, Yamaguchi H, Hiyama T, Kinoshita K, Hase N, Nakata K, Kondo A, Mogi M, Nakamura H IL-1beta-induced matrix metalloproteinase-13 is activated by a disintegrin and metalloprotease-28-regulated proliferation of human osteoblast-like cells. Exp Cell Res, 2014;323(1):165-77. 2014 [PMID: 24613731] (Bioassay, Human) Bioassay Human
Zhang Y, Mao X, Schwend T, Littlechild S, Conrad G Resistance of corneal RFUVA-cross-linked collagens and small leucine-rich proteoglycans to degradation by matrix metalloproteinases. Invest Ophthalmol Vis Sci, 2013;54(2):1014-25. 2013 [PMID: 23322569] (Enzyme Assay, Bovine) Enzyme Assay Bovine
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] (EnzAct, N/A) EnzAct N/A
Olivotto E, Vitellozzi R, Fernandez P, Falcieri E, Battistelli M, Burattini S, Flamigni F, Santi S, Borzi RM Chondrocyte hypertrophy and apoptosis induced by GROalpha require three-dimensional interaction with the extracellular matrix and a co-receptor role of chondroitin sulfate and are associated with the mitochondrial splicing variant of cathepsin B. J. Cell. Physiol., 2007;210(2):417-27. 2007 [PMID: 17096385] (ELISA Standard, N/A) ELISA Standard N/A

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Bioinformatics

Gene Symbol MMP13
Entrez
Uniprot