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SCP0007

Sigma-Aldrich

ADAM substrate

≥95% (HPLC), lyophilized

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About This Item

Formule empirique (notation de Hill):
C64H85N13O18S2
Poids moléculaire :
1388.57
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

product name

ADAM substrate, ≥95% (HPLC)

Pureté

≥95% (HPLC)

Forme

lyophilized

Composition

Peptide Content, ≥70%

Conditions de stockage

protect from light

Température de stockage

−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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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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.
Neumann U, Kubota H, Frei K, et al.
Analytical Biochemistry, 328, 166-173 (328)
Marcia L Moss et al.
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)-
Marcia L Moss et al.
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
Bernhard F Becker et al.
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

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