SouthBayBio

Z-Leu-Leu-Glu-AMC [Z-LLE-AMC]

CHF 204.00

In stock

SBB-PS0006-M0022 mgCHF 204.00

20S Immunoproteasome vs. 20S Constitutive Proteasome Activity: Z-LLE-AMC exhibits a high specific activity and preference for 20S constitutive proteasome compared to 20S immunoproteasome.

Specifications / Handling

More Information
Product Details
Synonyms	Proteasome Substrate II
Product Type	Chemical
Properties
Formula	C₃₅H₄₄N₄O₉
MW	664.8
Sequence	Z-Leu-Leu-Glu-7-amido-4-methylcoumarin
CAS	348086-66-8
Purity Chemicals	≥95% (HPLC)
Appearance	Lyophilized powder.
Solubility	Soluble in DMSO.
Declaration	Manufactured by South Bay Bio.
Other Product Data	Use: After preparing a stock solution in DMSO (≥10mM) store product at -20°C to -80°C. It is recommended to make multiple aliquots after the first thaw to ensure best performance. Caspase-like activity can be measured using a typical working concentration range from 10-50µM. Click here for a Typical Lot-specific Product Datasheet from the Original Manufacturer Our product description may differ slightly from the original manufacturers product datasheet.
InChi Key	FOYHOBVZPWIGJM-KCHLEUMXSA-N
Shipping and Handling
Shipping	BLUE ICE
Short Term Storage	+4°C
Long Term Storage	-20°C
Handling Advice	Avoid freeze/thaw cycles. Protect from light.
Use/Stability	Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS	Inquire
Product Specification Sheet
Datasheet	Download PDF

Product-specific References

Description

Z-LLE-AMC is a fluorogenic peptide substrate for measuring caspase-like activity of the proteasome. Hydrolysis of this substrate by the β1-subunit of the 20S proteasome is monitored by observing fluorescence at an Excitation wavelength of 345nm and Emission at 445nm. This substrate is specific to the constitutive proteasome and is not hydrolyzed efficiently by the immunoproteasome. 20S proteasome enzyme requires activation with 0.035% SDS in the assay buffer.

Product References

5,6,3',4'-Tetrahydroxy-7-methoxyflavone as a novel potential proteasome inhibitor: T.L. Chang, et al.; Planta Med. 76, 987 (2010)
Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S beta5-subunit: J. Blackburn, et al.; Biochem. J. 430, 461 (2010)

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