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ALX-200-310

Revised 27-Jun-06

Cathepsin G (human neutrophils)
PRODUCT LINE	Cancer
PRODUCT CATEGORY	Cathepsins

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-310-C100		100 µg	190.00 USD

Product Specification

MW:	~23.5kDa.
EC:	3.4.21.20
MERCK INDEX:	14: 1905
SOURCE/HOST:	Isolated from whole human blood (from single donors). Negative for HBSAG-, HCV- and HIV-antibodies.
PURITY:	≥95% (SDS-PAGE)
PURITY DETAIL:	Essentially salt free.
FORMULATION:	Lyophilized.
RECONSTITUTION:	Reconstitute with 50mM sodium acetate, pH 5.5, containing 150mM sodium chloride.
SPECIFIC ACTIVITY:	~2-4U/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Suc-Ala-Ala-Pro-Phe-pNA (1mM) per min. at 25°C in 160mM TRIS/HCl and 1.6M NaCl, pH 7.4.
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C

Product Specific Literature References

Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors: L.W. Heck, et al.; Anal. Biochem. 158, 217 (1986) Abstract

General Information

BACKGROUND/TECHNICAL INFORMATION

Swiss-Prot link P08311: Cathepsin G (human) (precursor)
AfCS Signalling Gateway link A000512: Cathepsin G (mouse)

Further Categories Containing This Product:

Natural Proteins • Enzymes

ALX-200-314

Revised 27-Jun-06

Cathepsin L (human)
PRODUCT LINE	Cancer
PRODUCT CATEGORY	Cathepsins

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-314-1		1 Vial	270.00 USD

Product Specification

MW:	~29kDa.
EC:	3.4.22.15
MERCK INDEX:	14: 1905
SOURCE/HOST:	Isolated from human liver. Negative for HBSAG-, HCV- and HIV-antibodies.
QUANTITY:	25µg
PURITY:	≥95% (SDS-PAGE)
FORMULATION:	Liquid. In 20mM malonate buffer, pH 5.5, containing 1mM EDTA and 400mM sodium chloride.
SPECIFIC ACTIVITY:	≥0.5U/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Z-Phe-Arg-AFC (Prod. No. ALX-260-129) per min. at 25°C in 400mM Na acetate, pH 5.5 with 4mM EDTA and 8mM DTT.
SHIPPING:	SHIPPED ON DRY ICE
LONG TERM STORAGE:	-80°C

Product Description

The most powerful of the lysosomal proteinases. It has a higher specific activity than cathepsin B and H in the degradation of a variety of physiological protein substrates.

Product Specific Literature References

Cathepsin B, Cathepsin H, and cathepsin L: A.J. Barrett & H. Kirschke; Methods Enzymol. 80 Pt C, 535 (1981) Abstract
Active center differences between cathepsins L and B: the S1 binding region: H. Kirschke, et al.; FEBS Lett 228, 128 (1988) Abstract
Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts: L.J. Joseph, et al.; J. Clin. Invest. 81, 1621 (1988) Abstract
The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation: T.Y. Nakagawa & A.Y. Rudensky; Immunol. Rev. 172, 121 (1999) Abstract
Proteases involved in MHC class II antigen presentation: J.A. Villadangos, et al.; Immunol. Rev. 172, 109 (1999) Abstract
Distinct roles of cathepsin K and cathepsin L in osteoclastic bone resorption: N. Furuyama & Y. Fujisawa; Endocr. Res. 26, 189 (2000) Abstract

General Information

BACKGROUND/TECHNICAL INFORMATION

May contain trace cathepsin B contaminant (<1.5U/mg protein using Z-Arg-Arg-β-NA as a substrate. One unit is defined as the amount of enzyme that hydrolyzes 1µmol of 2-naphtylamine per min. at 40°C, pH 6.0. Please note that the specific activity of pure cathepsin B is >200U/mg protein)

Swiss-Prot link P07711: Cathepsin L (human) (precursor)
AfCS Signalling Gateway link A000515: Cathepsin L (mouse)

Further Categories Containing This Product:

Natural Proteins • Enzymes

ALX-200-418

Revised 04-Sep-08

MMP-1 Proenzyme (human)
SYNONYMS	Collagenase (Type I) (human) Matrix Metalloproteinase 1 (human) Interstitial Collagenase (human)
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-418-C005		5 µg	182.00 USD

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)
SYNONYMS	Gelatinase A (human) Matrix Metalloproteinase 2 (human) Collagenase (72kDa Type IV) (human)
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-419-C005		5 µg	166.00 USD

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 K_mvalue 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-200-420

Revised 18-Mar-08

MMP-2/TIMP-2 Proenzyme Complex (human)
SYNONYMS	Matrix Metalloproteinase 2/Tissue Inhibitor of Metalloproteinase 2 Complex (human)
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-420-C005		5 µg	166.00 USD

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:

Tissue Inhibitors of Matrix Metalloproteinases [TIMPs] / Related Products • Natural Proteins • Enzymes

ALX-200-421

Revised 07-Nov-07

MMP-8 Proenzyme (human)
SYNONYMS	Matrix Metalloproteinase 8 (human) Neutrophil Collagenase (human)
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-421-C005		5 µg	136.00 USD

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-200-422

Revised 12-Nov-08

MMP-9 Proenzyme (human), Monomer
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

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-422-C005		5 µg	121.00 USD

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): no other MMP contaminants are detectable
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:	≥1’400mU/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-200-423

Revised 10-Feb-05

MMP-9 (human), Dimer
SYNONYMS	Matrix Metalloproteinase 9 (human), Dimer Collagenase (92kDa Type IV) (human), Dimer
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-423-C005		5 µg	151.00 USD

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.

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

MMP-9 hydrolyzes the extracellular matrix, e.g. collagen types IV, V and IX and gelatin.
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-200-424

Revised 04-Dec-04

MMP-9/Lipocalin Complex (human)
SYNONYMS	Matrix Metalloproteinase 9/Lipocalin Complex (human)
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	MMPs

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-200-424-C005		5 µg	166.00 USD

Product Specification

MW:	130kDa.
EC:	3.4.24.35 (MMP-9)
SOURCE/HOST:	Isolated from stimulated human neutrophil granulocytes (buffy coat). Disulfide-bridged complex of the monomer and a 25kDa protein of the lipocalin family. Requires activation.
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:	≥1'500mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol of Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0 (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)).
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
Progelatinase B forms from human neutrophils. complex formation of monomer/lipocalin with TIMP-1: H. Kolkenbrock, et al.; Biol. Chem. 377, 529 (1996) Abstract
Human neutrophil gelatinase and associated lipocalin in adult and localized juvenile periodontitis: U. Westerlund, et al.; J. Dent. Res. 75, 1553 (1996) Abstract

General Information

MMP-9 hydrolyzes the extracellular matrix, e.g. collagen types IV, V and IX and gelatin. Product 2