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ALX-200-422 Revised 07-Nov-07
MMP-9 Proenzyme (human), Monomer
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SYNONYMS Gelatinase B Proenzyme (human), Monomer
Matrix Metalloproteinase 9 Proenzyme (human), Monomer
Collagenase (92kDa Type IV) Proenzyme (human), Monomer
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-422-C005   5 µg 121.00 USD Add To Cart
Product Specification
MW: ~92kDa.
EC: 3.4.24.35
SOURCE/HOST: Isolated from stimulated human neutrophil granulocytes (buffy coat). Requires activation.
CONCENTRATION: 100µg/ml 
PURITY: ≥95% (SDS-PAGE, Western blot)
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7.0, containing 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% Brij 35, and 0.05% NaN3.
SPECIFIC ACTIVITY: ≥1’300mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
USE/STABILITY: Stable for 1 week when stored at +4°C and for serveral weeks when stored at -20°C.
HANDLING: Avoid freeze/thaw cycles.
Product Description
MMP-9 hydrolyzes the extracellular matrix, e.g. collagen types IV, V and IX and gelatin.
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
Progelatinase B forms from human neutrophils. complex formation of monomer/lipocalin with TIMP-1: H. Kolkenbrock, et al.; Biol. Chem. 377, 529 (1996) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) for 60-120 min. or 100µg/ml TPCK-trypsin for 30 min. at 37°C. If required trypsin can be inhibited by incubation with 1µl of 1mg/ml aprotinin solution for 10 min. at 25°C.
If working with MMP-9/TIMP-1 complexes, it is recommended to use stromelysin-1 (MMP-3) for activation. Incubation at 37°C for 2 hours at 40:1 (MMP-9:stromelysin-1) will remove only the propeptide to give the active form of the enzyme.

The active enzyme is inhibited by TIMP-1 (tissue inhibitor of matrix metalloproteinase-1) and by chelators of divalent cations like EDTA or o-phenantroline.

Swiss-Prot link P14780: MMP-9 (human) (precursor)
AfCS Signalling Gateway link A001479: MMP-9 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-418 Revised 23-Jul-07
MMP-1 Proenzyme (human)
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SYNONYMS Collagenase (Type I) (human)
Matrix Metalloproteinase 1 (human)
Interstitial Collagenase (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-418-C005   5 µg 182.00 USD Add To Cart
Product Specification
MW: ~56kDa.
EC: 3.4.24.7
SOURCE/HOST: Isolated from human rheumatoid synovial fibroblasts. Requires activation.
CONCENTRATION: 100µg/ml (Pierce-BCA).
PURITY: ≥90% (SDS-PAGE, Western blot)
PURITY DETAIL: No other MMP contaminants are detectable.
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7.0, 300mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35 and 0.05% sodium azide.
SPECIFIC ACTIVITY: ≥100mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0. APMA activation 1 hour at 37°C; enzyme dilution for assay 1:10/5-10µl for enzyme activity assay - incubation time 30min.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
Secreted forms of human neutrophil collagenase: K.A. Hasty, et al.; J. Biol. Chem. 261, 5645 (1986) Abstract; Full Text
Human fibroblast collagenase: glycosylation and tissue-specific levels of enzyme synthesis: S.M. Wilhelm, et al.; PNAS 83, 3756 (1986) Abstract
Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate: H. Nagase, et al.; Biochemistry 29, 5783 (1990) Abstract
Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin): K. Suzuki, et al.; Biochemistry 29, 10261 (1990) Abstract
Stepwise activation mechanisms of the precursors of matrix metalloproteinases 1 (tissue collagenase) and 3 (stromelysin): H. Nagase, et al.; Biomed. Biochim. Acta 50, 749 (1991) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix: B.K. Pilcher, et al.; J. Cell Biol. 137, 1445 (1997) Abstract
The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1): R. Vallon, et al.; Eur. J. Biochem. 244, 81 (1997) Abstract
General Information
MMP-1, the classical matrix metalloproteinase, is expressed by a large number of cell types. As an example, in basal keratinocytes migrating across the dermal matrix the enzyme is invariably expressed and cleaves fibrilliar collagen type I. It was shown that the interaction of the α2β1 integrin with dermal collagen mediates induction of MMP-1 in keratinocytes at the onset of healing and that the activity of MMP-1 is needed to initiate cell movement. The cleavage of dermal collagen provides keratinocytes with a mechanism to maintain their directionality during reepithelialization (Pilcher et al. 1997).
The MMP-1 zymogens of ~56/52kDa can be activated by a stepwise mechanism through which sequential processing events occur in the propeptide region. Both proenzymes can be activated by limited digestion with trypsin or by treatment with APMA generating their respective active enzyme forms of ~46/42kDa (Wilhelm et al. 1986).
BACKGROUND/TECHNICAL INFORMATION Activity:
We recommend to dilute this enzyme preparation at least 1:10 and to take 5µl or less for the determination of activity. Specific activity can be assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg (Dnp-peptide) (Masui et al.). Substrate concentration should be 0.5mg/ml in buffer 50mM TRIS-HCl, pH 7.0, 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35, 0.05% sodium azide, containing 0.05mg/ml albumin. One unit MMP catalyzes the hydrolysis of 1µmol Dnp-peptide/min at 37°C and pH 7.0.
We recommend to employ the fluorogenic substrate (7-Methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-β-Dnp-L-α,β-diaminopropionyl-Ala-Arg-NH2) (Knight et al. 1992). The hydrolysis of the Gly-Leu bond separates the highly fluorescent (7-Methoxycoumarin-4-yl)acetyl group from the 2,4-dinitrophenyl resulting in an increase of fluorogenic intensity. The substrate should be kept as a 9.15mM stock solution in DMSO (10mg/ml). In the assay the substrate concentration should be ~25mM. The assay can be performed in a 96-well microtiter plate (200µl per well) suitable for fluorogenic measurements (excitation wavelength of 328nm; emission wavelength of 393nm).

Activation:
Do not dilute enzyme for activation! Activation is required by trypsin (2µl trypsin; 1mg/ml) for 10-20 min. at 37°C and stopped by the addition of 10µl trypsin-inhibitor (2mg/ml) or aprotinin or TLCK. Activation can also be done by 2mM (final concentration) APMA for 60 min. at 37°C.

Inhibitors:
Only  the activated and not the latent forms of wild-type MMP-1 protein is able to form a complex with TIMP-1. Quite in contrast to MMP-2 (gelatinase A) and MMP-9 (gelatinase B), in MMP-1 the C-terminal hemopexin domain does not interact with TIMP-1. The integrity of the catalytic domain of MMP-1 and its ability to bind Zn2+ is absolutely required for complex formation with TIMP-1, which further underlines the importance of this region for proper regulation of enzymatic activity of MMP-1 (Vallon et al. 1997). Therefore, the enzyme is also inhibited by chelators of divalent cations like EDTA or o-phenantroline.

Swiss-Prot link P03956: MMP-1 (human)
AfCS Signalling Gateway link A001461: MMP-1 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-419 Revised 20-Mar-08
MMP-2 Proenzyme (human)
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SYNONYMS Gelatinase A (human)
Matrix Metalloproteinase 2 (human)
Collagenase (72kDa Type IV) (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-419-C005   5 µg 166.00 USD Add To Cart
Product Specification
MW: ~72kDa.
EC: 3.4.24.24
SOURCE/HOST: Isolated from human rheumatoid synovial fibroblasts. Requires activation.
CONCENTRATION: 40µg/ml (Pierce-BCA).
PURITY: ≥90% (SDS-PAGE, Western blot)
PURITY DETAIL: No other MMP contaminants are detectable.
FORMULATION: Liquid. In 50mM TRIS-HCl pH 7.0, containing 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35 0.05% sodium azide.
SPECIFIC ACTIVITY: ≥850mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.
APPLICATION: Immunogen for antibody generation, control in immunoassays and for characterizing interactions with MMP inhibitors.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase: H. Kolkenbrock, et al.; Biol. Chem. 378, 71 (1997) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION

Activity:
Specific activity can be assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg (Dnp-peptide) (Masui et al.). Substrate concentration should be 0.5mg/ml in 50mM TRIS-HCl, pH 7.0, 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% sodium azide, 0.05% BRIJ35, containing 0.05mg/ml albumine. One unit MMP catalyzes the hydrolysis of 1µmol Dnp-peptide/min. at 37°C and pH 7.0.
Alternatively the fluorogenic substrate Substrat (7-Methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-N-ß-Dnp-L-(α,ß-diaminopropionyl)Ala-Arg-NH2 (Knight et al. 1992) can be used. Hydrolysis of the Gly-Leu bond separates the highly fluorescent (7-Methoxycoumarin-4-yl)acetyl group from the 2,4-dinitrophenyl resulting in an increase of fluorogenic intensity. The Km value for the gelatinase A is 7.0x105M-1s-1. Substrate should be kept as a  9.15mM stock solution in DMSO (10mg/ml). In the assay the substrate concentration should be ~25µM. The assay can be performed in a 96-well microtiter plate (100/200µl per well) suitable for fluorogenic measurements (Ex 328 nm; Em 393 nm).

Activation:
Requires activation by 2mM (final concentration) AMPA or 1mM mersalic acid for 60-120 min. at 37°C. We do not recommend to use trypsin for activation! Do not dilute enzyme for activation!

Inhibitors:
Activated enzyme is inhibited by tissue inhibitors of matrix metalloproteinase-2 (TIMP-2) and by chelators of divalent cations like EDTA or o-phenanthroline.

Swiss-Prot link P08253: MMP-2 (human) (precursor)
AfCS Signalling Gateway link A001471: MMP-2 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-201-095 Revised 05-Aug-08
MMP-2 Proenzyme (human) (recombinant)
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SYNONYMS Progelatinase A (human) (recombinant)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-201-095-C010   10 µg 350.00 USD Add To Cart
Product Specification
MW: ~72kDa.
EC: 3.4.24.24
SOURCE/HOST: Produced in Sf9 cells.
CONCENTRATION: 0.2mg/ml
PURITY: ≥95% (SDS-PAGE)
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7.0, 200mM NaCl, 5mM CaCl2, 0.05% Brij-35.
SPECIFIC ACTIVITY: ≥120mU/mg protein after AMPA activation. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 per min. at 37°C, pH 7.5.
SHIPPING: SHIPPED ON DRY ICE
SHORT TERM STORAGE: -20°C
LONG TERM STORAGE: -80°C
USE/STABILITY: Stable for several weeks when stored at -20°C.
HANDLING: Avoid freeze/thaw cycles.
Product Description
Active MMP-2 is used to study the degradations of proteins of the extracellular matrix, including fibrillar collagens. MMP-2 is inhibited by tissue inhibitors of matrix metalloproteinases (TIMP), α2-macroglobulin and by chelators of divalent cations as EDTA or o-phenanthroline.
Product Specific Literature References
[1] A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION

Activation of MMP-2 proenzyme and measurement of catalytic activity

1 Preparation and stability of solutions:
∙ APMA-solution: 40mM p-aminophenyl mercuric acetate (APMA) in DMSO. Store at -20°C.
∙ Peptide hydrolysis buffer: 50mM TRIS-HCl, pH 7.5, 150mM NaCl, 5mM CaCl2, 0.025% Brij 35. Solution
  is stable for several weeks at 4°C.
∙ Stock solution of peptide substrate: 100µM solution of Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 in 20%
  DMSO. Store at -20°C.
∙ Stock solution of unquenched peptide: 10µM solution of Mca-Pro-Leu-NH2 in 20% DMSO. Store at -20°C.

2 Activation:
An aliquot of 19.5μl MMP-2 proenzyme is mixed with 0.5µl APMA solution and is incubated for 60 min. at 37°C.

3 Assay protocol:
The activity of MMP-2 is measured fluorimetrically with a synthetic internally quenched fluorescent substrate according to Knight et al. [1].
An excitation wavelength of 328nm and an emission wavelength of 393nm are set in an appropriate fluorimeter. The instrument is calibrated with the unquenched peptide Mca-Pro-Leu at a concentration corresponding to between 2 and 10% hydrolysis of the protease substrate. Kinetic reactions are conveniently carried out in a constant volume of 2.5ml. The substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg is diluted in peptide hydrolysis buffer to a concentration of  0.8µM and equilibrated at a temperature of 37°C. Aliquots of 1 to 2µl of the activation mixture are than added and the increase in fluorescence is recorded over a time interval between 2 and 12 minutes. Activity units per ml enzyme solution are calculated according to the following equation:

Activity (U/ml) = (CMca-Pro-Leu/FMca-Pro-Leu) x (ΔFMca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg/Venzyme) x Vtotal

CMca-Pro-Leu: Concentration of Mca-Pro-Leu used for calibration of the fluorimeter (µmoles/ml).
FMca-Pro-Leu: Fluorescence of Mca-Pro-Leu at the concentration CMca-Pro-Leu used for fluorimeter calibration.
ΔFMca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg: Change in fluorescence during peptide hydrolysis per min.
Vtotal: Volume of peptide hydrolysis reaction (2.5ml).
Venzyme: Volume of added enzyme (0.001 to 0.002ml).

Due to autoproteolytic activity minor bands of activated enzyme may be visible in the preparation.

Swiss-Prot link P08253: MMP-2 (human)
AfCS Signalling Gateway link A001471: MMP-2 (mouse)
Further Categories Containing This Product:
Enzymes • Recombinant Proteins/Fusion Proteins
 
 
ALX-200-420 Revised 18-Mar-08
MMP-2/TIMP-2 Proenzyme Complex (human)
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SYNONYMS Matrix Metalloproteinase 2/Tissue Inhibitor of Metalloproteinase 2 Complex (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-420-C005   5 µg 166.00 USD Add To Cart
Product Specification
EC: 3.4.24.24 (MMP-2)
SOURCE/HOST: Isolated from human rheumatoid synovial fibroblasts. Requires activation.
CONCENTRATION: ~100µg/ml
PURITY: ≥95% (SDS-PAGE, Western blot)
PURITY DETAIL: No other MMP contaminants are detectable.
FORMULATION: Liquid. In 50mM TRIS-HCl pH 7.0, 200mM sodium chloride, 5mM CaCl2, 1µM ZnCl2, 0.05% NaN3 and 0.05% BRIJ 35.
SPECIFIC ACTIVITY: ≥30mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH 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: Do always keep the enzyme on ice.
HANDLING: Avoid freeze/thaw cycles.
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor: H. Kolkenbrock, et al.; Eur. J. Biochem. 198, 775 (1991) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase: H. Kolkenbrock, et al.; Biol. Chem. 378, 71 (1997) Abstract
General Information
MMP-2 and TIMP-2 form a stable, but non-covalent 1:1 stoichiometric complex. The complex inhibits active matrix MMP's like collagenases and gelatinases and shows proteolytic activity after activation with APMA (4-aminophenylmercury acetate).
BACKGROUND/TECHNICAL INFORMATION Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) or 1mM mersalylic acid for 60-120 min. at 37°C. Do not use trypsin for activation! Do not dilute the enzyme for activation!

The active enzyme is inhibited by TIMP-1 (tissue inhibitor of matrix metalloproteinase-1) and by chelators of divalent cations like EDTA or o-phenantroline.

Swiss-Prot link: MMP-2 (human) (precursor) (P08253), TIMP-2 (human) (precursor) (P16035)
Further Categories Containing This Product:
Natural Proteins • Tissue Inhibitors of Matrix Metalloproteinases [TIMPs]/Related Products • Enzymes
 
 
ALX-201-042 Revised 09-Mar-06
MMP-3 (Catalytic Domain) (human) (recombinant)
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SYNONYMS Stromelysin-1 (human) (recombinant)
Matrix Metalloproteinase 3 (Catalytic Domain) (human) (recombinant)
Transin-1 (human) (recombinant)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-201-042-C005   5 µg 197.00 USD Add To Cart
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:
Enzymes • Recombinant Proteins/Fusion Proteins
 
 
ALX-200-421 Revised 07-Nov-07
MMP-8 Proenzyme (human)
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SYNONYMS Matrix Metalloproteinase 8 (human)
Neutrophil Collagenase (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-421-C005   5 µg 136.00 USD Add To Cart
Product Specification
MW: ~85kDa.
EC: 3.4.24.34
SOURCE/HOST: Isolated from stimulated human neutrophil granulocytes (buffy coat). Requires activation.
CONCENTRATION: 100µg/ml
PURITY: ≥90% (SDS-PAGE)
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7.0, containing 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ 35, and 0.05% sodium azide.
SPECIFIC ACTIVITY: ≥60mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
USE/STABILITY: Stable for 1 week when stored at +4°C and for serveral weeks when stored at -20°C.
HANDLING: Avoid freeze/thaw cycles.
Product Description
MMP-8 is a glycoprotein containing complex N-linked oligosaccharides. It hydrolyzes type I over type II, and III collagens. Activated MMP-8 is inhibited by TIMP-1 (Prod. No. ALX-200-426).
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
Secreted forms of human neutrophil collagenase: K.A. Hasty, et al.; J. Biol. Chem. 261, 5645 (1986) Abstract; Full Text
Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase: S.K. Mallya, et al.; Biochemistry 29, 10628 (1990) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION

Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) or 1mM mersalylic acid for 60 min. at 37°C. Alternatively use 0.1mM PCMB (p-chloromercuribenzoate) or 10µg/ml trypsin for 20 min. at 25°C; PCMB is substantially more effective.

The active enzyme is inhibited by TIMP-1 (tissue inhibitor of matrix metalloproteinase-1) and by chelators of divalent cations like EDTA or o-phenantroline.

Swiss-Prot link P22894: MMP-8 (human) (precursor)
AfCS Signalling Gateway link A001478: MMP-8 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-430 Revised 08-Dec-04
MMP-9 Proenzyme (human), Monomer
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PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-430-C010   10 µg 560.00 USD Add To Cart
Product Specification
MW: ~92kDa.
EC: 3.4.24.35
SOURCE/HOST: Isolated from human blood. Requires activation.
FORMULATION: Liquid. Contains 0.05% sodium azide.
SPECIFIC ACTIVITY: 350-450mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 per min. at 37°C, pH7.5.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P14780: MMP-9 (human) (precursor)
AfCS Signalling Gateway link A001479: MMP-9 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-423 Revised 10-Feb-05
MMP-9 (human), Dimer
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SYNONYMS Matrix Metalloproteinase 9 (human), Dimer
Collagenase (92kDa Type IV) (human), Dimer
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-423-C005   5 µg 151.00 USD Add To Cart
Product Specification
MW: ~220kDa.
EC: 3.4.24.35
SOURCE/HOST: Isolated from stimulated human neutrophil granulocytes (buffy coat). Disulfide-bridged MMP-9 homodimer.
PURITY: ≥95% (SDS-PAGE, Western blot)
FORMULATION: Liquid. 5µg protein in 200mM NaCl, 50mM Tris-HCl pH 7.0, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35, and 0.05% sodium azide.
SPECIFIC ACTIVITY: ≥2'000mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0 (C.C. Knight, et al.; FEBS Lett. 296, 263 (1992)).
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.