Search Thermo Fisher Scientific
Certificates
SDS
Citations & References (22)
Invitrogen™
DQ™ Collagen, type I From Bovine Skin, Fluorescein Conjugate
The fluorogenic DQ™ collagen can be used to directly monitor collagenase activity. DQ™ substrates are analogs of the natural substrateRead more
| Catalog Number | Quantity |
|---|---|
| D12060 | 1 mg |
Catalog number D12060
Price (EUR)
610,00
Each
-
Quantity:
1 mg
Price (EUR)
610,00
Each
The fluorogenic DQ™ collagen can be used to directly monitor collagenase activity. DQ™ substrates are analogs of the natural substrate that have an excessive number of fluorescent dyes attached so that the fluorescence signal is almost non-existent. This quenching of the signal is caused by the close proximity of the dyes on the intact substrate. The enzyme-driven hydrolysis of the substrate results in separation of the dye results in separation of the dye molecules from one another and the fluorescence signal increases.
See User Manual for solubility instructions.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Product LineDQ™
Quantity1 mg
Shipping ConditionRoom Temperature
SubstrateProtease Substrate
Detection MethodFluorescence
FormLyophilized
Substrate PropertiesProtein-Based Substrate
Target EnzymeMetalloproteinase
Unit SizeEach
Contents & Storage
Store in freezer (-5°C to -30°C) and protect from light.
Have questions about this product? Ask our AI assisted search.
This is an AI-powered search and may not always get things right. You can help us make it better with a thumbs up or down on individual answers or by selecting the “Give feedback" button. Your search history and customer login information may be retained by Thermo Fisher and processed in accordance with our
Privacy Notice.
Customers who viewed this item also viewed
Documents & Downloads
Certificates
Search by lot number or partial lot number
Lot #Certificate TypeDateCatalog Number(s)
2991657Certificate of AnalysisSep 17, 2024D12060
2841633Certificate of AnalysisFeb 05, 2024D12060
2488883Certificate of AnalysisAug 01, 2022D12060
2513464Certificate of AnalysisMay 20, 2022D12060
2306796Certificate of AnalysisMar 29, 2021D12060
5 results displayed, search above for a specific certificate
Safety Data Sheets
SDSProduct Information
Citations & References (22)
Search citations by name, author, journal title or abstract text
Citations & References
Abstract
The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.
Journal:J Biol Chem
PubMed ID:17065155
'The hydrolysis of collagen (collagenolysis) is one of the committed steps in extracellular matrix turnover. Within the matrix metalloproteinase (MMP) family distinct preferences for collagen types are seen. The substrate determinants that may guide these specificities are unknown. In this study, we have utilized 12 triple-helical substrates in combination with
Type I collagen contains at least 14 cryptic fibronectin binding sites of similar affinity.
Journal:Arch Biochem Biophys
PubMed ID:12413494
'There is uncertainty in the literature regarding the number and location of fibronectin binding sites on denatured collagen. Although most attention has focused on a single site near the collagenase-sensitive region of each alpha chain, there is evidence for additional sites in other regions. We treated bovine type I collagen
TGF-beta1 + EGF-initiated invasive potential in transformed human keratinocytes is coupled to a plasmin/MMP-10/MMP-1-dependent collagen remodeling axis: role for PAI-1.
Journal:Cancer Res
PubMed ID:19383899
'The phenotypic switching called epithelial-to-mesenchymal transition is frequently associated with epithelial tumor cell progression from a comparatively benign to an aggressive, invasive malignancy. Coincident with the emergence of such cellular plasticity is an altered response to transforming growth factor-beta (TGF-beta) as well as epidermal growth factor (EGF) receptor amplification. TGF-beta
Vascular endothelial growth factor-C and C-C chemokine receptor 7 in tumor cell-lymphatic cross-talk promote invasive phenotype.
Journal:Cancer Res
PubMed ID:19118020
'Most carcinomas spread to distant sites through lymphatic vessels. Several preclinical and clinical studies have shown a positive correlation between the incidence of lymph node metastasis and secretion of the lymphatic growth factor vascular endothelial growth factor-C (VEGF-C) by tumor cells, suggesting tumor lymphangiogenesis as an escape mechanism. However, recent
Metabolic mapping of proteinase activity with emphasis on in situ zymography of gelatinases: review and protocols.
Journal:J Histochem Cytochem
PubMed ID:15150280
'Proteases are essential for protein catabolism, regulation of a wide range of biological processes, and in the pathogenesis of many diseases. Several techniques are available to localize activity of proteases in tissue sections or cell preparations. For localization of the activity of matrix metalloproteinases, in situ zymography was introduced some
22 total citations