539175
Proteasome Inhibitor IV
The Proteasome Inhibitor IV controls the biological activity of Proteasome. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.
Synonym(s):
Proteasome Inhibitor IV, Z-GPFL-CHO
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About This Item
Empirical Formula (Hill Notation):
C30H38N4O6
Molecular Weight:
550.65
UNSPSC Code:
12352200
Assay:
≥90% (HPLC)
Form:
lyophilized solid
Quality level:
Storage condition:
OK to freeze, protect from light
Quality Level
assay
≥90% (HPLC)
form
lyophilized solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, protect from light
color
white
solubility
DMSO: 5 mg/mL
shipped in
ambient
storage temp.
−20°C
General description
A 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.
Biochem/physiol Actions
Cell permeable: no
Primary Target
branched chain amino acid preferring,small neutral amino acid preferring, chymotrypsin-like activities
branched chain amino acid preferring,small neutral amino acid preferring, chymotrypsin-like activities
Product does not compete with ATP.
Reversible: no
Target Ki: 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
Packaging
Packaged under inert gas
Preparation Note
Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Other Notes
Oberdorf, J., et al. 2001. Biochemistry40, 13397.
Cardozo, C., et al. 1999. Biochemistry38, 9768.
Eleuteri, A.M., et al. 1997. J. Biol. Chem.272, 11824.
Orlowski, M., et al. 1997. Biochemistry36, 13946.
Vinitsky, A., et al. 1994. J. Biol. Chem.269, 29860.
Cardozo, C., et al. 1999. Biochemistry38, 9768.
Eleuteri, A.M., et al. 1997. J. Biol. Chem.272, 11824.
Orlowski, M., et al. 1997. Biochemistry36, 13946.
Vinitsky, A., et al. 1994. J. Biol. Chem.269, 29860.
Z-Gly-Pro-Phe-Leu-CHO
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Related Content
J Oberdorf et al.
Biochemistry, 40(44), 13397-13405 (2001-10-31)
Misfolded proteins in the endoplasmic reticulum (ER) are degraded by N-terminal threonine proteases within the 26S proteasome. Each protease is formed by an activated beta subunit, beta5/X, beta1/Y, or beta2/Z, that exhibits chymotrypsin-like, peptidylglutamyl-peptide hydrolyzing, or trypsin-like activity, respectively. Little
A M Eleuteri et al.
The Journal of biological chemistry, 272(18), 11824-11831 (1997-05-02)
Amino acid sequencing of subunits of the multicatalytic proteinase complex (MPC) isolated from bovine spleen showed an almost complete replacement of the X, Y, and Z subunits, constitutively expressed in most tissues, by the interferon-gamma-inducible LMP7, LMP2, and MECL1 subunits.
A Vinitsky et al.
The Journal of biological chemistry, 269(47), 29860-29866 (1994-11-25)
Evidence indicates that a component of the multicatalytic proteinase complex (MPC) that preferentially cleaves bonds after branched chain amino acids (BrAAP) is a major factor responsible for the protein-degrading activity of the MPC. We report here the synthesis of substrate-related