DQ™ Gelatin From Pig Skin, Fluorescein Conjugate - Special Packaging
DQ™ Gelatin From Pig Skin, Fluorescein Conjugate - Special Packaging
Zitierungen und Referenzen (50)
Invitrogen™

DQ™ Gelatin From Pig Skin, Fluorescein Conjugate - Special Packaging

Unsere DQ-Gelatine ist ein fluorogenes Substrat, das in vitro zur Erkennung von Protease-Aktivität mit hoher Empfindlichkeit verwendet werden kann. DiesesWeitere Informationen
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KatalognummerMenge
D120545 × 1 mg
Katalognummer D12054
Preis (EUR)
568,00
Each
Zum Warenkorb hinzufügen
Menge:
5 × 1 mg
Preis (EUR)
568,00
Each
Zum Warenkorb hinzufügen
Unsere DQ-Gelatine ist ein fluorogenes Substrat, das in vitro zur Erkennung von Protease-Aktivität mit hoher Empfindlichkeit verwendet werden kann. Dieses Substrat, das früher nur in unserem beliebten EnzChek Gelatinase/Collagenase-Assay-Kit (E-12055) erhältlich war, besteht aus hoch gequenchter, Fluorescein-markierter Gelatine. Nach dem proteolytischen Verdau tritt seine leuchtende, grüne Fluoreszenz auf, die zur Messung der enzymatischen Aktivität verwendet werden kann. Die Steigerung der Fluoreszenz kann mit einem Fluoreszenz-Mikrotiterplatten-Lesegerät oder Fluorometer überwacht werden.
Nur für Forschungszwecke. Nicht zur Verwendung bei diagnostischen Verfahren.
Specifications
ProduktlinieDQ
Menge5 × 1 mg
VersandbedingungRaumtemperatur
SubstratProtease-Substrat
NachweisverfahrenFluoreszent
FormPulver
Substrate PropertiesProtein-basiertes Substrat
Target EnzymeMetalloproteinase
Unit SizeEach
Inhalt und Lagerung
Bei -5 bis -30 °C lagern und vor Licht schützen.

Zitierungen und Referenzen (50)

Zitierungen und Referenzen
Abstract
Gelatin in situ zymography on fixed, paraffin-embedded tissue: zinc and ethanol fixation preserve enzyme activity.
Authors:Hadler-Olsen E, Kanapathippillai P, Berg E, Svineng G, Winberg JO, Uhlin-Hansen L,
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 ... More
Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2.
Authors:Deshane J, Garner CC, Sontheimer H
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 ... More
Authentic matrix vesicles contain active metalloproteases (MMP). a role for matrix vesicle-associated MMP-13 in activation of transforming growth factor-beta.
Authors:D'Angelo M, Billings PC, Pacifici M, Leboy PS, Kirsch T
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 ... More
Molecular proximity of seprase and the urokinase-type plasminogen activator receptor on malignant melanoma cell membranes: dependence on beta1 integrins and the cytoskeleton.
Authors:Artym VV, Kindzelskii AL, Chen WT, Petty HR
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 ... More
Pancreatic trypsin increases matrix metalloproteinase-9 accumulation and activation during acute intestinal ischemia-reperfusion in the rat.
Authors:Rosário HS, Waldo SW, Becker SA, Schmid-Schönbein GW
Journal:Am J Pathol
PubMed ID:15111317
'Ischemia-reperfusion of the intestine produces a set of inflammatory mediators, the origin of which has recently been shown to involve pancreatic digestive enzymes. Matrix metalloproteinase-9 (MMP-9) participates in a variety of inflammatory processes including myocardial, hepatic, and pancreatic ischemia-reperfusion. In the present study, we explore the role of neutrophil-derived MMP-9 ... More
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