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Assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥70%
storage condition
protect from light
storage temp.
−20°C
Amino Acid Sequence
NMe-Phe-Lys-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Dabcyl-Lys-NH2
Application
ADAM substrate containing the fluorophore quencher Dabcy is used in FRET applications for detection of metalloprotease activity. DABCYL is a popular acceptor for developing FRET-based protease substrates. DABCYL dyes are often paired with EDANS in FRET-based fluorescent probes.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Analytical biochemistry, 366(2), 144-148 (2007-06-06)
In this paper we describe novel fluorescent substrates for the human ADAM family members ADAM17, ADAM10, ADAM8, and ADAM12 that have good specificity constants and are useful for high-throughput screening of inhibitors. The fluorescence resonance energy transfer substrates contain a
Combinatorial chemistry & high throughput screening, 13(4), 358-365 (2009-12-18)
Fluorescence resonance energy transfer substrates were designed and tested as substrates for ADAM9. The donor/quencher pair used were 5-carboxy fluorescein (Fam) and 4-(4-dimethyl-aminophenylazo)benzoyl (Dabcyl) since they have been well studied sensitive fluorescent probes. The peptides based on precursor TNF-alpha, Dabcyl-Ser-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Lys(Fam)-
Biological chemistry, 383(11), 1821-1826 (2003-01-18)
Tumor necrosis factor-alpha (TNFalpha) is presumably shed from cell membranes by TNFalpha-cleaving enzyme (TACE). The peptides SPLAQAVRSSSR and Dabcyl-LAQAVRSSSR-Edans, each encompassing the cleavage sequence of pro-TNFalpha recognized by TACE, were applied to intact umbilical vein endothelium (HUVEC), peripheral blood leukocytes
Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme.
Analytical Biochemistry, 328, 166-173 (328)
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