DQ™ Gelatin From Pig Skin, Fluorescein Conjugate - Special Packaging
Citations & References (50)
Invitrogen™
DQ™ Gelatin From Pig Skin, Fluorescein Conjugate - Special Packaging
Our DQ gelatin is a fluorogenic substrate that can be used to detect protease activity in vitro with high sensitivity.Read more
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Catalog Number
Quantity
D12054
5 x 1 mg
Catalog number D12054
Price (CNY)
5,445.00
Each
Add to cart
Quantity:
5 x 1 mg
Price (CNY)
5,445.00
Each
Add to cart
Our DQ gelatin is a fluorogenic substrate that can be used to detect protease activity in vitro with high sensitivity. This substrate, formerly available only in our popular EnzChek Gelatinase/Collagenase Assay Kit (E-12055), consists of highly quenched, fluorescein-labeled gelatin. Upon proteolytic digestion, its bright, green fluorescence is revealed and can be used to measure enzymatic activity. The fluorescence increase can be monitored with a fluorescence microplate reader or fluorometer.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Product LineDQ
Quantity5 x 1 mg
Shipping ConditionRoom Temperature
SubstrateProtease Substrate
Detection MethodFluorescence
FormPowder
Substrate PropertiesProtein-Based Substrate
Target EnzymeMetalloproteinase
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.
Citations & References (50)
Citations & References
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.
'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