CC1048
MMP-9, human, proform
Sinonimo/i:
Progelatinase B, 92 kDa Type IV Collagenase
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Codice UNSPSC:
12352200
eCl@ss:
32160405
NACRES:
NA.41
Prodotti consigliati
Origine biologica
human
Saggio
>95% (total protein)
Forma fisica
liquid
Attività specifica
>1200 mU/mg (specific activity of activated MMP-9 after trypsin activation)
Produttore/marchio commerciale
Chemicon®
Concentrazione
0.2 mg/mL
N° accesso NCBI
N° accesso UniProt
Condizioni di spedizione
dry ice
Informazioni sul gene
human ... MMP9(4318)
Descrizione generale
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
Applicazioni
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.
Definizione di unità
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
Stato fisico
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.
Stoccaggio e stabilità
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.
Risultati analitici
MMP-9 monomer appears as a major band at 92 kDa in non-reducing SDS-PAGE
Note legali
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Esclusione di responsabilità
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.
Codice della classe di stoccaggio
12 - Non Combustible Liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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)
R W Thompson et al.
The Journal of clinical investigation, 96(1), 318-326 (1995-07-01)
Abdominal aortic aneurysms (AAA) are characterized by disruption and degradation of the elastic media, yet the elastolytic proteinases involved and their cellular sources are undefined. We examined if 92-kD gelatinase, an elastolytic matrix metalloproteinase, participates in the pathobiology of AAA.
Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin.
Goldberg, G I, et al.
The Journal of Biological Chemistry, 267, 4583-4591 (1992)
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.