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 E. coli is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).
Human MMP3 expressed in E.coli
CAT# CSC-CTK0376-10 (10 μg); CAT# CSC-CTK0376-50 (50 μg)
Greater than 98% as determined by SDS-PAGE and HPLC analyses.
MMP-3 activity was measured by its ability to cleave a chromogenic peptide MMP-3 substrate at room temperature. At an MMP-3 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 75 minutes.
Less than 1 EU/μg.
Sterile-filtered through a 0.2 micron filter and ly ophilized from 10 mM sodium phosphate buffer (pH 7.5), 0.1% CHAPS, 0.1 mM calcium chloride.
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0.5 - 1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored dessicated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at –20°C. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze / thaw cycles.
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