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ActoFactor™ Recombinant Human Matrix metallopeptidase 3 (HEK)
- Specification
Cat.No.
CSC-CTK0370
Description
MMP-3 enzyme is also known as Stromelysin-1 or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL-1 beta.|Human recombinant MMP-3 produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus. It has an MW of 52 kDa and has been purified by using proprietary chromatographic techniques.
Species
Human
Product Overview
Human MMP3 expressed in HEK cells
Molecular Mass
52 kDa
Size
CAT# CSC-CTK0370-10 (10 μg); CAT# CSC-CTK0370-50 (50 μg)
Expression System
HEK cells
Purity
Greater than 95% as determined by SDS-PAGE analysis.
Activity
The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca- RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is >150 pmoles/min/μg.
Endotoxin Level
N/A
Formulation
Sterile-filtered (0.2 μm), colorless solution in Tris, NaCl and Brij35.
Reconstitution
Please centrifuge product briefly before opening vial. The protein solution can be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid repeated freeze-thaw cycles.
Citation Guidance
If you use this products in your scientific publication, it should be cited in the publication as: Creative Bioarray cat no. If your paper has been published, please click here to submit the PubMed ID of your paper to get a coupon.
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