ALEXIS Biochemicals: MMP-3 (Catalytic Domain) (human) (recombinant)

ALX-201-042

Revised 09-Mar-06

MMP-3 (Catalytic Domain) (human) (recombinant)
SYNONYMS	Stromelysin-1 (human) (recombinant) Matrix Metalloproteinase 3 (Catalytic Domain) (human) (recombinant) Transin-1 (human) (recombinant)
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-201-042-C005		5 µg	197.00 USD

Product Specification

MW:	~22kDa.
EC:	3.4.24.17
SOURCE/HOST:	Produced in E. coli.
CONCENTRATION:
PURITY DETAIL:	No other MMP contaminants are detectable.
FORMULATION:	Liquid. In 50mM Tris-HCl, pH 7.5, containing 10mM CaCl₂, 1µM ZnCl₂ and 0.05% sodium azide.
SPECIFIC ACTIVITY:	≥900mU/mg protein (H. Nagase, et al; J. Biol. Chem. 269, 20952 (1994)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(DNP)-NH₂ per min. at 37°C, pH 7.0.
SHIPPING:	SHIPPED ON DRY ICE
SHORT TERM STORAGE:	-20°C
LONG TERM STORAGE:	-80°C
USE/STABILITY:	Stable for several weeks when stored at at -20°C and for at least 1 week when stored at at +4°C.
HANDLING:	Avoid freeze/thaw cycles.

Product Description

Highly purified recombinant enzyme containing the 22kDa catalytic domain of MMP-3.

Product Specific Literature References

Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes: G. Murphy, et al.; Biochem. J. 248, 265 (1987) Abstract
Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase: A. Ito & H. Nagase; Arch. Biochem. Biophys. 267, 211 (1988) Abstract
Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9: Y. Ogata, et al.; J. Biol. Chem. 267, 3581 (1992) Abstract; Full Text
A trypsin sensitive stromelysin isolated from rheumatoid synovial fluid is an activator for matrix metalloproteinases: H. Kolkenbrock, et al.; Eur. J. Clin. Chem. Clin. Biochem. 31, 625 (1993) Abstract
Matrix metalloproteinase-3 (stromelysin-1). Identification as the cartilage acid metalloprotease and effect of pH on catalytic properties and calcium affinity: S.M. Wilhelm, et al.; J. Biol. Chem. 268, 21906 (1993) Abstract; Full Text
Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3): H. Nagase, et al.; J. Biol. Chem. 269, 20952 (1994) Abstract; Full Text

General Information

BACKGROUND/TECHNICAL INFORMATION

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. The activating process generates an active 45kDa species which converts easily to a highly active 28kDa form. Product ALX-201-042 displays the same activity as the 28kDa form.

Swiss-Prot link P08254: MMP-3 (human) (precursor)
AfCS Signalling Gateway link A001476: MMP-3 (mouse)

Further Categories Containing This Product:

Recombinant Proteins / Fusion Proteins • Enzymes

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