CC1048
MMP-9, human, proform
Synonym(e):
Progelatinase B, 92 kDa Type IV Collagenase
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About This Item
UNSPSC-Code:
12352200
eCl@ss:
32160405
NACRES:
NA.41
Empfohlene Produkte
Biologische Quelle
human
Assay
>95% (total protein)
Form
liquid
Spezifische Aktivität
>1200 mU/mg (specific activity of activated MMP-9 after trypsin activation)
Hersteller/Markenname
Chemicon®
Konzentration
0.2 mg/mL
NCBI-Hinterlegungsnummer
UniProt-Hinterlegungsnummer
Versandbedingung
dry ice
Angaben zum Gen
human ... MMP9(4318)
Allgemeine Beschreibung
When measured with the peptide substrate dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg [Masui et al., 1977] the specific activity of MMP-9 monomer
Anwendung
ACTIVATION:
An aliquot of 10 μL MMP-9 monomer is mixed with 20 μL trypsin solution (see below) and activation buffer in a total volume of 100 μL. The mixture is incubated for 20 min at 37°C. Thereafter trypsin is inhibited by addition of 10 μL aprotinin solution.
Trypsin solution: 0.50 mg TPCK-trypsin/mL activation buffer. The solution is stored in aliquots at -20°C.
Activation Buffer: 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl2.
Aprotinin solution: 1 mg aprotinin/mL activation buffer. The solution is stored at -20°C.
An aliquot of 10 μL MMP-9 monomer is mixed with 20 μL trypsin solution (see below) and activation buffer in a total volume of 100 μL. The mixture is incubated for 20 min at 37°C. Thereafter trypsin is inhibited by addition of 10 μL aprotinin solution.
Trypsin solution: 0.50 mg TPCK-trypsin/mL activation buffer. The solution is stored in aliquots at -20°C.
Activation Buffer: 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl2.
Aprotinin solution: 1 mg aprotinin/mL activation buffer. The solution is stored at -20°C.
Einheitendefinition
Specific Activity: where 1 U is the activity that hydrolyzes 1 mmol peptide (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dpa-Ala-Arg) within 1 minute under the assay conditions described by Knight ,et al
Physikalische Form
Provided as a liquid in 50 mM Tris-HCl, pH 7.0, 200 mM NaCl, 5 mM CaCl2, ,1 μM ZnCl2, 0.05% Brij-35, 0.05% NaN3.
Lagerung und Haltbarkeit
Maintain frozen at -70°C in undiluted aliquots. The enzyme may be stored at -20°C for several without significant loss of activity. Repeated freezing and thawing should be avoided.
Hinweis zur Analyse
MMP-9 monomer appears as a major band at 92 kDa in non-reducing SDS-PAGE
Rechtliche Hinweise
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Haftungsausschluss
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Lagerklassenschlüssel
12 - Non Combustible Liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.
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M(r) 92,000 type IV collagenase is increased in plasma of patients with colon cancer and breast cancer.
Zucker, S, et al.
Cancer Research, 53, 140-146 (1993)
Synthetic substrates for vertebrate collagenase.
Masui, Y, et al.
Biochemical Medicine, 17, 215-221 (1977)
Matrix metalloproteinases (MMP-2 and MMP-9) of the oral cavity: cellular origin and relationship to periodontal status.
Makela, M, et al.
Journal of Dental Research, 73, 1397-1406 (1994)
I E Collier et al.
Genomics, 9(3), 429-434 (1991-03-01)
The 72- and 92-kDa type IV collagenases are members of a group of secreted zinc metalloproteases. Two members of this family, collagenase and stromelysin, have previously been localized to the long arm of chromosome 11. Here we assign both of
Secretion of collagenolytic enzymes by human polymorphonuclear leukocytes.
Hibbs, M S, et al.
Collagen and Related Research, 4, 467-477 (1984)
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