(Suc-Leu-Leu-Val-Tyr)2-Rhodamine 110

(Suc-LLVY)2-Rhodamine is a fluorogenic substrate for the chymotrypsin – like activity of the 20S and 26S proteasomes. Working concentrations of this substrate is 20-100 µM. The released Rhodamine 110 fluorescence can be detected by a fluorimeter or plate reader at excitation/emission of 495 nm/520nm, respectively. Compared to AMC, Rhodamine 110 is excited at longer wavelength that can significantly enhance the signal/noise ratio. This substrate is extremly valuable for screening small chemical inhibitors of proteasomes by avoiding the interference from chemical compound autofluorescence that often occurs at shorter wavelengths around UV or near-UV regions.

When used to determine proteasome activity in cell lysates, cell lysates that are pre-treated with a proteasome inhibitor such as MG132, PS341 or epoxomicin can be used to determine the fluorescence contributed by other cellular proteases that cleave this substrate. Readings from proteasome inhibitor-treated lysates should be subtracted.

Additional Information

Product Name: (Suc-Leu-Leu-Val-Tyr)2-Rhodamine 110
Also Known As: (Suc-LLVY)2-Rhodamine 110
Catalog No.: G1110
Size: 2 mg
Molecular Weight: 1507.7 Da
Species: N/A
Source: Synthetic
Stock: Powder
Concentration: N/A
Quality Assurance: >98% by HPLC and NMR
Storage: Eligible for room temperature shipping. Store at -20°C upon receiving; avoid multiple freeze-thaw cycles after dissolving in DMSO.
PDF Data Sheet: Download PDF datasheet, MSDS
NCBI RefSeq: N/A
Image(s): No
Shipping Method: Room temperature shipping
References: No

Details

(Suc-LLVY)2-Rhodamine is a fluorogenic substrate for the chymotrypsin – like activity of the 20S and 26S proteasomes. The working concentrations of this substrate is 20-100 µM. The released Rhodamine 110 fluorescence can be detected by a fluorimeter or plate reader at excitation/emission of 495 nm/520nm, respectively. Compared to AMC, Rhodamine 110 is excited at longer wavelength that can significantly enhance the signal/noise ratio. This substrate is extremly valuable for screening small chemical inhibitors of proteasomes by avoiding the interference from chemical compound autofluorescence that often occurs at shorter wavelengths around UV or near UV regions. When used to determine proteasome activity in cell lysates, cell lysates that are pre-treated with a proteasome inhibitor such as MG132, PS341 or epoxomicin should be used to determine the fluorescence contributed by other cellular proteases that cleave this substrate. Readings from proteasome inhibitor-treated lysates can be subtracted as background.