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Citas y referencias (46)
Invitrogen™
EnzChek™ Gelatinase/Collagenase Assay Kit, 250-2,000 assays
El kit de ensayo de gelatinasa/colagenasa EnzChek proporciona un método fluorimétrico sensible, práctico y rápido para medir la actividad deMás información
| Número de catálogo | Cantidad |
|---|---|
| E12055 | 1 kit |
Número de catálogo E12055
Precio (CLP)
500.991
Each
Cantidad:
1 kit
Precio (CLP)
500.991
Each
El kit de ensayo de gelatinasa/colagenasa EnzChek proporciona un método fluorimétrico sensible, práctico y rápido para medir la actividad de la gelatinasa o colagenasa en sistemas enzimáticos purificados, lisados de células/tejidos o para detectar inhibidores en un formato de alto rendimiento. El sustrato del kit EnzChek es nuestro conjugado de gelatina DQ etiquetada con fluoresceína que está altamente etiquetado para que la señal de fluorescencia se desactive hasta que la digestión enzimática produzca fragmentos muy fluorescentes. Este sustrato también está disponible por separado del kit (D-12054).
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Método de detecciónIntensidad de la fluorescencia
Cantidad1 kit
Condiciones de envíoTemperatura ambiente
Propiedades de sustratoSustrato basado en proteínas
Tipo de sustratoSustrato de colagenasa⁄gelatinasa
Enzima dianaGelatinasa⁄Colagenasa
Para utilizar con (aplicación)Ensayo de gelatinasa/colagenasa
Línea de productosEnzChek
Tipo de productoEnsayo de gelatinasa⁄colagenasa
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Citations & References (46)
Citations & References
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