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Citations et références (46)
Invitrogen™
EnzChek™ Gelatinase/Collagenase Assay Kit, 250-2,000 assays
Le kit de dosage de gélatinase/collagénase EnzChek fournit une méthode fluorométrique sensible, pratique et rapide pour mesurer l’activité de laAfficher plus
| Référence | Quantité |
|---|---|
| E12055 | 1 kit |
Référence E12055
Prix (EUR)
649,65
Precio exclusivo en nuestra web
764,00Économisez 114,35 (15%)
Each
Quantité:
1 kit
Prix (EUR)
649,65
Precio exclusivo en nuestra web
764,00Économisez 114,35 (15%)
Each
Le kit de dosage de gélatinase/collagénase EnzChek fournit une méthode fluorométrique sensible, pratique et rapide pour mesurer l’activité de la gélatinase ou de la collagénase dans les systèmes enzymatiques purifiés, les lysats de cellules/tissus ou les inhibiteurs de criblage dans un format à haut débit. Le substrat du kit EnzChek est notre conjugué de gélatine DQ marqué par fluorescéine qui est hautement marqué de manière que le signal de fluorescence soit éteint jusqu’à ce que la digestion enzymatique produise des fragments hautement fluorescents. Ce substrat est également disponible séparément du kit (D-12054).
Usage exclusivement réservé à la recherche. Ne pas utiliser pour des procédures de diagnostic.
Spécifications
Méthode de détectionIntensité de fluorescence
Quantité1 kit
Conditions d’expéditionTempérature ambiante
Propriétés du substratSubstrat à base de protéines
Type de substratSubstrat de la gélatinase / collagénase
Enzyme cibleGélatinase / collagénase
À utiliser avec (application)Dosage de gélatinase/collagénase
Gamme de produitsEnzChek
Type de produitTest de la gélatinase⁄collagénase
Unit SizeEach
Contenu et stockage
Stocker au congélateur (entre -5°C et -30°C) à l’abri de la lumière.
Citations et références (46)
Citations et références
Abstract
Gelatin in situ zymography on fixed, paraffin-embedded tissue: zinc and ethanol fixation preserve enzyme activity.
Journal:J Histochem Cytochem
PubMed ID:19755718
In situ zymography is a method for the detection and localization of enzymatic activity in tissue sections. This method is used with frozen sections because routine fixation of tissue in neutral-buffered formalin inhibits enzyme activity. However, frozen sections present with poor tissue morphology, making precise localization of enzymatic activity difficult
Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2.
Journal:J Biol Chem
PubMed ID:12454020
'Primary brain tumors (gliomas) have the unusual ability to diffusely infiltrate the normal brain thereby evading surgical treatment. Chlorotoxin is a scorpion toxin that specifically binds to the surface of glioma cells and impairs their ability to invade. Using a recombinant His-Cltx we isolated and identified the principal Cltx receptor
Authentic matrix vesicles contain active metalloproteases (MMP). a role for matrix vesicle-associated MMP-13 in activation of transforming growth factor-beta.
Journal:J Biol Chem
PubMed ID:11145962
'Matrix vesicles (MV) play a key role in the initiation of cartilage mineralization. Although many components in these microstructures have been identified, the specific function of each component is still poorly understood. In this study, we show that metalloproteases (MMP), MMP-2, -9, and -13 are associated with MV isolated from
Effective antiprotease-antibiotic treatment of experimental anthrax.
Journal:BMC Infect Dis
PubMed ID:15819985
'BACKGROUND: Inhalation anthrax is characterized by a systemic spread of the challenge agent, Bacillus anthracis. It causes severe damage, including multiple hemorrhagic lesions, to host tissues and organs. It is widely believed that anthrax lethal toxin secreted by proliferating bacteria is a major cause of death, however, the pathology of
Molecular proximity of seprase and the urokinase-type plasminogen activator receptor on malignant melanoma cell membranes: dependence on beta1 integrins and the cytoskeleton.
Journal:Carcinogenesis
PubMed ID:12376466
'Previous studies have shown that several proteolytic enzymes are associated with membrane protrusions at the leading edge of migrating tumor cells. In this study we demonstrate that seprase and the urokinase plasminogen activator receptor (uPAR), co-localize in the plasma membrane of LOX malignant melanoma cells. Cells were labeled with fluorochrome-conjugated