AdipoGen Life Sciences

Ac-Pro-Ala-Leu-AMC

CHF 65.00
In stock
AG-CP3-0036-M0011 mgCHF 65.00
AG-CP3-0036-M0055 mgCHF 140.00
AG-CP3-0036-M02525 mgCHF 560.00
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Product Details
Synonyms Ac-PAL-AMC; Immunoproteasome Substrate
Product Type Chemical
Properties
Formula

C26H34N4O6

MW 498.6
Sequence

Acetyl-Pro-Ala-Leu-7-amido-4-methylcoumarin

CAS 1431362-79-6
Purity Chemicals ≥97%
Appearance Lyophilized powder.
Solubility Soluble in DMSO.
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.

InChi Key BWJPVHDZSJFFDM-NDXORKPFSA-N
Smiles O=C(C)N1CCC[C@H]1C(N[C@@H](C)C(N[C@@H](CC(C)C)C(NC2 =CC=C(C(C)=CC(O3)=O)C3=C2)=O)=O)=O
Shipping and Handling
Shipping AMBIENT
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 Download PDF
Product Specification Sheet
Datasheet Download PDF
Description
  • Ac-PAL-AMC is a fluorogenic peptide substrate for measuring caspase-like activity of the immunoproteasome. 
  • Hydrolysis of this substrate by the β1i/LMP2-subunit of the immunoproteasome is monitored by observing fluorescence at an Excitation wavelength of 345nm and Emission at 445nm. 
  • This substrate is specific to the immunoproteasome and is not hydrolyzed efficiently by the constitutive proteasome.
Product References
  1. Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S β5-subunit: C. Blackburn, et al.; Biochem. J. 430, 461 (2010)
  2. PSMB9 codon 60 polymorphisms have no impact on the activity of the immunoproteasome catalytic subunit B1i expressed in multiple types of solid cancer: J.E. Park, et al.; PloS one 8, e73732 (2013)
  3. Inhibitors of the immunoproteasome: current status and future directions: Z. Miller, et al.; Curr. Pharm. Des. 19, 4140 (2013)
  4. Development and characterization of selective immunoproteasome inhibitors: C. Dubiella; Diss. Universitaet Muenchen (2015)
  5. Cleavage specificity of Mycobacterium tuberculosis ClpP1P2 protease and identification of novel peptide substrates and boronate inhibitors with anti-bacterial activity: T. Akopian, et al.; J. Biol. Chem. 290, 11008 (2015)
  6. Discovery of highly selective inhibitors of the immunoproteasome low molecular mass polypeptide 2 (LMP2) subunit: H.W.B. Johnson, et al.; ACS Med. Chem. Lett. 8, 413 (2017)
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