Proteasome Inhibitor IV

Name: Proteasome Inhibitor IV
Brand: MM

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

Select a Size

All Photos(1)

About This Item

Empirical Formula (Hill Notation):

C₃₀H₃₈N₄O₆

Molecular Weight:

550.65

UNSPSC Code:

12352200

Product Name

Proteasome Inhibitor IV, The Proteasome Inhibitor IV controls the biological activity of Proteasome. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.

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

Quality Level

100

Packaging

Packaged under inert gas

Biochem/physiol Actions

Cell permeable: no

Primary Target
branched chain amino acid preferring,small neutral amino acid preferring, chymotrypsin-like activities

Product does not compete with ATP.

Reversible: no

Target K_i: 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

Disclaimer

Toxicity: Standard Handling (A)

General description

A tetrapeptide aldehyde that acts as a highly selective and potent proteasomal inhibitor (K_i = 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.

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.

Z-Gly-Pro-Phe-Leu-CHO

Preparation Note

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Bovine spleen multicatalytic proteinase complex (proteasome). Replacement of X, Y, and Z subunits by LMP7, LMP2, and MECL1 and changes in properties and specificity.

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.

Redundancy of mammalian proteasome beta subunit function during endoplasmic reticulum associated degradation.

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

Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes.

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

Reactions of [14C]-3,4-dichloroisocoumarin with subunits of pituitary and spleen multicatalytic proteinase complexes (proteasomes).

M Orlowski et al.

Biochemistry, 36(45), 13946-13953 (1997-12-31)

Exposure to [14C]-3,4-dichloroisocoumarin (DCI) of multicatalytic proteinase complexes (MPC) isolated from bovine pituitary and spleen leads to label incorporation into several beta-type subunits, to rapid inactivation of the chymotrypsin-like (ChT-L) activity, and to a slower inactivation of other activities of

Components of the bovine pituitary multicatalytic proteinase complex (proteasome) cleaving bonds after hydrophobic residues.

C Cardozo et al.

Biochemistry, 38(30), 9768-9777 (1999-07-28)

Two catalytic components of the multicatalytic proteinase complex (MPC, proteasome) designated as chymotrypsin-like (ChT-L) and branched chain amino acid preferring (BrAAP) cleave bonds after hydrophobic amino acids. The possible involvement of the ChT-L and peptidylglutamyl-peptide hydrolyzing (PGPH) activities in the