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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-200-422 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-200-423 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.
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)
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SYNONYMS Matrix Metalloproteinase 9/Lipocalin Complex (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-424-C005   5 µg 166.00 USD Add To Cart
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 200-424 represents the 130kDa disulfide-bridged complex of the monomer and a 25kDa protein of the lipocalin family and displays homology with the α2-macroglobulin-related protein from rats. The human MMP-9/lipocalin complex was shown to be associated with adult and localized juvenile periodontitis.
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link: MMP-9 (human) (precursor) (P1480), Lipocalin (human) (precursor) (P80188)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-425 Revised 04-Mar-05
MMP-9/Lipocalin/TIMP-1 Complex (human)
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SYNONYMS Matrix Metalloproteinase 9/Lipocalin/Tissue Inhibitor of Metalloproteinase 1 Complex (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-425-C005   5 µg 166.00 USD Add To Cart
Product Specification
EC: 3.4.24.35 (MMP-9)
SOURCE/HOST: Isolated from stimulated human neutrophil granulocytes (buffy coat). 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: ≥400mU/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 (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 Description
This product represents the ternary complex of the MMP-9 monomer, lipocalin and TIMP-1 and behaves like the progelatinase B/TIMP-1 complex, that inhibits active MMP's and, after activation acts as a gelatinase with reduced activity.
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: MMP-9 (human) (precursor) (P14780), Lipocalin (human) (precursor) (P80188), TIMP-1 (human) (precursor) (P01033)
Further Categories Containing This Product:
Natural Proteins • Tissue Inhibitors of Matrix Metalloproteinases [TIMPs] / Related Products • Enzymes
 
 
ALX-200-426 Revised 26-Jun-08
TIMP-1 (human)
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SYNONYMS Tissue Inhibitor of Metalloproteinase 1 (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY Tissue Inhibitors of Matrix Metalloproteinases [TIMPs] / Related Products
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ALX-200-426-C005   5 µg 197.00 USD Add To Cart
Product Specification
MW: ~28kDa.
SOURCE/HOST: Isolated from stimulated human neutrophils. The secreted protein consists of 184 amino acids, six disulfide bonds and two glycosylation sites containing N-linked oligosaccharides.
CONCENTRATION: 80µg/ml
PURITY: ≥92% (SDS-PAGE, Western blot)
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7.0, 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ 35 and 0.05% sodium azide.
SHIPPING: SHIPPED ON DRY ICE
SHORT TERM STORAGE: -20°C
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
Product Description
Specific inhibitor of matrix metalloproteinases (MMPs). It has no activity on mammalian membrane metalloproteinases, procollagen peptidase or on bacterial metalloproteinases such as thermolysin.
Product Specific Literature References
The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor: T.E. Cawston, et al.; Biochem. J. 211, 313 (1983) Abstract
Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes: G. Murphy, et al.; Biochem. J. 248, 265 (1987) Abstract
Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family: W.G. Stettler-Stevenson, et al.; J. Biol. Chem. 264, 17374 (1989) Abstract; Full Text
Generation and activity of the ternary gelatinase B/TIMP-1/LMW-stromelysin-1 complex: H. Kolkenbrock, et al.; Biol. Chem. 376, 495 (1995) 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
Shedding of the Transferrin Receptor Is Mediated Constitutively by an Integral Membrane Metalloprotease Sensitive to Tumor Necrosis Factor alpha Protease Inhibitor-2: M. Kaup, et al.; J. Biol. Chem. 277, 38494 (2002) Abstract; Full Text
General Information
BACKGROUND/TECHNICAL INFORMATION

Note: It is recommended to perform a preincubation of ~20 min. at 37°C to allow formation of the enzyme-inhibitor complex.

Swiss-Prot link P01033: TIMP-1 (human) (precursor)
AfCS Signalling Gateway link A002285: TIMP-1 (mouse)
Further Categories Containing This Product:
Natural Proteins
 
 
ALX-200-427 Revised 25-Apr-08
TIMP-2 (human)
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SYNONYMS Tissue Inhibitor of Metalloproteinase 2 (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY Tissue Inhibitors of Matrix Metalloproteinases [TIMPs] / Related Products
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ALX-200-427-C005   5 µg 212.00 USD Add To Cart
Product Specification
MW: ~21kDa (non-reduced); ~24kDa (reduced) (SDS-PAGE).
SOURCE/HOST: Isolated from human fibroblasts.
CONCENTRATION: 40μg/ml
PURITY: ≥90% (SDS-PAGE, Western blot)
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7, containing 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ 35 and 0.05% sodium azide.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
Product Images
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Product Description
Glycoprotein that belongs to a family which takes part in the activation and regulation of the MMP-activity. Forms a non-covalent stoichiometric complex with latent and active MMP's. Inhibits the activities of MMP-1, MMP-2, MMP-12 and transin.
Product Specific Literature References
Purification and characterization of a two-chain form of tissue inhibitor of metalloproteinases (TIMP) type 2 and a low molecular weight TIMP-like protein: K. Miyazaki, et al.; J. Biol. Chem. 268, 14387 (1993) Abstract; Full Text
Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4: J. Greene, et al.; J. Biol. Chem. 271, 30375 (1996) Abstract; Full Text
Shedding of the Transferrin Receptor Is Mediated Constitutively by an Integral Membrane Metalloprotease Sensitive to Tumor Necrosis Factor alpha Protease Inhibitor-2: M. Kaup, et al.; J. Biol. Chem. 277, 38494 (2002) Abstract; Full Text
General Information
BACKGROUND/TECHNICAL INFORMATION

Note: It is recommended to perform a preincubation of about 20min at 37°C which allows the formation of the enzyme-inhibitor complex.

Swiss-Prot link P16035: TIMP-2 (human) (precursor)
AfCS Signalling Gateway A002286: TIMP-2 (mouse)
Further Categories Containing This Product:
Natural Proteins
 
 
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-201-006 Revised 04-Sep-08
N-Acetyl-eglin C (recombinant)
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PRODUCT LINE Cancer
PRODUCT CATEGORY Cathepsin Inhibitors
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ALX-201-006-MC01   0.1 mg 95.00 USD Add To Cart
ALX-201-006-MC05   0.5 mg 380.00 USD Add To Cart
ALX-201-006-M001   1 mg 670.00 USD Add To Cart
Product Specification
SEQUENCE: Ac-Thr-Glu-Phe-Gly-Ser-Glu-Leu-Lys-Ser-Phe-Pro-Glu-Val-Val-Gly-Lys-Thr-Val-Asp-Gln-Ala-Arg-Glu-Tyr-Phe-Thr-Leu-His-Tyr-Pro-Gln-Tyr-Asn-Val-Tyr-Phe-Leu-Pro-Glu-Gly-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-Asp-Arg-Val-Arg-Val-Phe-Tyr-Asn-Pro-Gly-Thr-Asn-Val-Val-Asn-His-Val-Pro-His-Val-Gly-OH
FORMULA: C377H552N96O107
MW: 8141.1
CAS NUMBER: 96380-69-7
SOURCE/HOST: Produced in E. coli.
PURITY: ≥97% (HPLC)
APPEARANCE: White to off-white powder.
SOLUBILITY: Soluble in water.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
Product Description
Eglin C was originally isolated from the leech Hirudo medicinalis [1]. Recombinant N-acetyl-eglin C is a 70 amino acid peptide with identical biological activity to native eglin C. An effective inhibitor of chymotrypsin and subtilisin as well as of leukocyte elastase and cathepsin G.
Product Specific Literature References
[1] Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis: U. Seemüller, et al.; Hoppe-Seyler's Z. Physiol. Chem. 361, 1841 (1980) Abstract
[2] A large fragment approach to DNA synthesis: total synthesis of a gene for the protease inhibitor eglin c from the leech Hirudo medicinalis and its expression in E. coli: H. Rink, et al.; Nucl. Acids Res. 12, 6369 (1984) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P01051: Eglin C (Hirudo medicinalis)
Further Categories Containing This Product:
Recombinant Proteins / Fusion Proteins • Proteases Other Products
 
 
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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