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Recombinant Human MMP-15/MT2-MMP Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 916-MP

R&D Systems, part of Bio-Techne
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916-MP-010

Key Product Details

Source

NS0

Accession #

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human MMP-15/MT2-MMP protein
Glu47-Pro565 (Arg128Pro) (Arg129Gly), with a C-terminal 5-His tag

Purity

>70%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Glu47

Predicted Molecular Mass

61 kDa

SDS-PAGE

60-65 kDa, reducing conditions

Activity

Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 (Catalog # ES010).
The specific activity is >200 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

916-MP
Formulation Supplied as a 0.2 μm filtered solution in MES, NaCl and Glycerol.
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.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: MMP-15/MT2-MMP

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. They play critical roles in tissue remodeling, angiogenesis, tumor invasion, and rheumatoid arthritis (1). MMP-15, also known as MT2-MMP, is a membrane-type MMP that is expressed in many tumor tissues including urothelial carcinoma, oral cancer, ovarian carcinoma, melanoma, and astrocytoma (2). Structurally, MMP-15 consists of the following domains:a pro domain containing a furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplasmic tail (1). Recombinant Human (rh) MMP-15, consists of the pro domain, catalytic domain, hinge region and hemopexin-like domain. The pro domain contains the mutations R128P and R129G, which prevent activation by furin cleavage. Activation of rhMMP-15 is possible by treatment with rhTrypsin 3 as described in the Activity Assay Protocol.

References

  1. Takino, T. et al. (1995) J. Biol. Chem. 270:23013.
  2. Yana I. and M. Seiki (2004) Handbook of Proteolytic Enzymes (ed. Barrett, et al.) p. 549-551, Academic Press, San Diego.

Long Name

Matrix Metalloproteinase 15/Membrane Type 2 MMP

Alternate Names

MMP15, MT2-MMP

Entrez Gene IDs

4324 (Human)

Gene Symbol

MMP15

UniProt

Additional MMP-15/MT2-MMP Products

Product Documents for Recombinant Human MMP-15/MT2-MMP Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human MMP-15/MT2-MMP Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

For research use only

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