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208771

Sigma-Aldrich

Calpain Substrate III, Fluorogenic

A fluorogenic FRET peptide with a substrate sequence that is optimized for calpain-1 and -2.

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Synonym(s):
Calpain Substrate III, Fluorogenic, (DABCYL)-TPLK~SPPPSPR-(EDANS)
Empirical Formula (Hill Notation):
C80H114N20O18S
Molecular Weight:
1675.95

Quality Level

assay

≥98% (HPLC)

form

lyophilized solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
protect from light

color

red

solubility

water: 1 mg/mL
DMSO: 5 mg/mL

fluorescence

λex 320 nm
λem 480 nm

shipped in

wet ice

storage temp.

−20°C

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This Item
208772208748208773
Sigma-Aldrich

208771

Calpain Substrate III, Fluorogenic

Sigma-Aldrich

208748

Calpain-1 Substrate, Fluorogenic

form

lyophilized solid

form

lyophilized solid

form

lyophilized solid

form

lyophilized solid

manufacturer/tradename

Calbiochem®

manufacturer/tradename

Calbiochem®

manufacturer/tradename

Calbiochem®

manufacturer/tradename

Calbiochem®

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

solubility

water: 1 mg/mL, DMSO: 5 mg/mL

solubility

DMSO: 5 mg/mL

solubility

DMSO: 1 mg/mL

solubility

DMSO: 5 mg/mL

General description

A fluorogenic FRET peptide with a substrate sequence that is optimized for calpain-1 and -2 based on 106 known cleavage sites. It is cleaved by mammalian calpains with a much better efficacy (kcat/Kmx10-2 (M-1s-1) = 69.8, 38.5, 20.0, 6.81, 3.58, 0.05, and <0.05 for calpain-2, trypsin, papain, calpain-B, calpain-A, chymotrypsin, and cathepsin-B, respectively) and kinetically superior to other commonly used calpain substrates, such as LY-AMC and α-spectrin cleavage site-based substrate. Has been used successfully in monitoring calpain activity in whole Drosophila S2 cells (cellular incorporation achieved with a lipofection reagent) and in COS-7 cell lysate.
A fluorogenic FRET peptide with a substrate sequence that is optimized for calpain-1 and -2 based on 106 known cleavage sites. It is cleaved by mammalian calpains with higher efficiency (kcat/Kmx10-2 (M-1s-1) = 69.8, 38.5, 20.0, 6.81, 3.58, 0.05, and <0.05 for calpain-2, trypsin, papain, calpain-B, calpain-A, chymotrypsin, and cathepsin-B, respectively). It is kinetically superior to other commonly used calpain substrates, such as LY-AMC (Cat. No. 208731) and α-spectrin cleavage site-based substrate (Cat. No. 208748). Has been used successfully in monitoring calpain activity in intact Drosophila S2 cells (cellular incorporation achieved with a lipofection reagent) and in COS-7 cell lysate.

Biochem/physiol Actions

Cell permeable: no
Primary Target
Substrate sequence that is optimized for calpain-1 and -2
Product does not compete with ATP.
Reversible: no
kcat/Kmx10-2 (M-1s-1) = 69.8, 38.5, 20.0, 6.81, 3.58, 0.05, and <0.05 for calpain-2, trypsin, papain, calpain-B, calpain-A, chymotrypsin, and cathepsin-B, respectively

Packaging

Packaged under inert gas

Warning

Toxicity: Irritant (B)

Sequence

DABCYL-Thr-Pro-Leu-Lys~Ser-Pro-Pro-Pro-Ser-Pro-Arg-EDANS

Physical form

Supplied as a trifluoroacetate salt.

Reconstitution

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Other Notes

Tompa, P., et al. 2004. J. Biol. Chem.279, 20775.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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