Millipore Sigma Vibrant Logo
Attention: We have moved. EMD Millipore products are no longer available for purchase on emdmillipore.com.Learn More

539175 Proteasome Inhibitor IV - Calbiochem

Overview

Replacement Information

Key Specifications Table

Empirical Formula
C₃₀H₃₈N₄O₆

Products

Catalog NumberPackaging Qty/Pack
539175-5MG Plastic ampoule 5 mg
Description
OverviewA tetrapeptide aldehyde that acts as a highly selective and potent proteasomal inhibitor (Ki = 1.5 µM for branched chain amino acid preferring, 2.3 µM for small neutral amino acid preferring, and 40.5 µM for chymotrypsin-like activities; IC50 = 3.1 µM for peptidyl-glutamyl peptide hydrolyzing activity). Shown to be a weak inhibitor of trypsin-like proteasomal activity.
Catalogue Number539175
Brand Family Calbiochem®
SynonymsZ-GPFL-CHO
References
ReferencesOberdorf, J., et al. 2001. Biochemistry 40, 13397.
Cardozo, C., et al. 1999. Biochemistry 38, 9768.
Eleuteri, A.M., et al. 1997. J. Biol. Chem. 272, 11824.
Orlowski, M., et al. 1997. Biochemistry 36, 13946.
Vinitsky, A., et al. 1994. J. Biol. Chem. 269, 29860.
Product Information
ATP CompetitiveN
FormWhite lyophilized solid
Hill FormulaC₃₀H₃₈N₄O₆
Chemical formulaC₃₀H₃₈N₄O₆
ReversibleN
Quality LevelMQ100
Applications
Biological Information
Primary Targetbranched chain amino acid preferring,small neutral amino acid preferring, chymotrypsin-like activities
Primary Target K<sub>i</sub>1.5 µM, 2.3 µM, and 40.5 µM against branched chain amino acid preferring, small neutral amino acid preferring, and chymotrypsin-like activities of proteasomes, respectively
Purity≥90% by HPLC
Physicochemical Information
Cell permeableN
Peptide SequenceZ-Gly-Pro-Phe-Leu-CHO
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage -20°C
Protect from Light Protect from light
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Packaging Information
Packaged under inert gas Packaged under inert gas
Transport Information
Supplemental Information
Specifications

Documentation

Proteasome Inhibitor IV - Calbiochem SDS

Title

Safety Data Sheet (SDS) 

Proteasome Inhibitor IV - Calbiochem Certificates of Analysis

TitleLot Number
539175

References

Reference overview
Oberdorf, J., et al. 2001. Biochemistry 40, 13397.
Cardozo, C., et al. 1999. Biochemistry 38, 9768.
Eleuteri, A.M., et al. 1997. J. Biol. Chem. 272, 11824.
Orlowski, M., et al. 1997. Biochemistry 36, 13946.
Vinitsky, A., et al. 1994. J. Biol. Chem. 269, 29860.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision15-October-2009 RFH
SynonymsZ-GPFL-CHO
DescriptionA tetrapeptide aldehyde that acts as a highly selective and potent proteasomal inhibitor (Ki = 1.5 µM for branched chain amino acid preferring, 2.3 µM for small neutral amino acid preferring, and 40.5 µM for chymotrypsin-like activities; IC50 = 3.1 µM for peptidyl-glutamyl peptide hydrolyzing activity). Shown to be a weak inhibitor of trypsin-like proteasomal activity.
FormWhite lyophilized solid
Intert gas (Yes/No) Packaged under inert gas
Chemical formulaC₃₀H₃₈N₄O₆
Peptide SequenceZ-Gly-Pro-Phe-Leu-CHO
Purity≥90% by HPLC
SolubilityDMSO (5 mg/ml)
Storage Protect from light
-20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Toxicity Standard Handling
ReferencesOberdorf, J., et al. 2001. Biochemistry 40, 13397.
Cardozo, C., et al. 1999. Biochemistry 38, 9768.
Eleuteri, A.M., et al. 1997. J. Biol. Chem. 272, 11824.
Orlowski, M., et al. 1997. Biochemistry 36, 13946.
Vinitsky, A., et al. 1994. J. Biol. Chem. 269, 29860.