While the detection of cathepsin
activity plays a crucial role in the research of a number of pathological
processes, the sensitivity of traditional cathepsin assay kits has been significantly
hampered by autofluorescence interference at lower wavelengths. AnaSpec is
pleased to introduce a brilliant new solution.
The SensoLyte™ 520 Cathepsin
D Activity Assay Kit offers ultra-sensitive Cathepsin D detection at the industry’s
longest wavelength. Leveraging AnaSpec’s proprietary
fluorescence technology, the SensoLyte™ 520 Cathepsin D Activity Assay Kit
incorporates a FRET substrate that fluoresces at a much higher wavelength
than standard substrates. The higher wavelength
fluorescence results in cathepsin detection that avoids autofluorescence interference
from cell components and test compounds.
The FRET substrate in the SensoLyte™ 520 Cathepsin D Activity Assay
Kit utilizes a unique 5-FAM/QXL™520 FRET pair (Ex/Em=490
nm/520 nm upon cleavage). The sequence of the FRET substrate
is derived from the cleavage site of Cathepsin D. In the intact
FRET peptides the fluorescence of donors is quenched by the acceptors. When
active Cathepsin D cleaves FRET substrate into two separate fragments, the
fluorescence of the donor is recovered, and can be monitored.
AnaSpec also offers the SensoLyte™ 390 Cathepsin D Activity Assay Kit
that uses a traditional Mca/Dnp FRET peptide for measurement of enzyme activity
(Ex/Em=330 nm/390 nm upon cleavage)
Cathepsin is a protease that breaks apart other proteins
found in many types of cells. There are at least 12 members of the cathepsin
family which are distinguished by their structure and the proteins that they
cleave. Cathepsin D is the lysosomal aspartic
proteinase implicated in intracellular protein degradation.
Request AnaSpec’s FRET
Technology brochure today. Click here
390 Cathepsin D Activity Assay Kit (Ex/Em = 330 nm/390 nm)
Inhibitors & Peptide
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237, 167 (2006).
3. Davidson, Y. et al, J Neurol Neurosurg
Psychiat.77, 515 (2006).
4. Laurent-Matha, V. et al, J Cell
Biol. 168,489 (2005).
5. Simon, DI. et al, Biochemistry
33, 6555 (1994).
6. Baechle, D. et al, J Peptide Sci.
11, 166 (2005).
7. Yasuda, Y. et al, J Biochem.
125, 1137 (1999)