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Merck

P8465

Protease Inhibitor Cocktail

lyophilized powder, for the inhibition of serine, cysteine, aspartic, metalloproteases and aminopeptidases, for use with bacterial cell extracts, lyophilized powder

Synonyme(s) :

Protease inhibitor

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A propos de cet article

UNSPSC Code:
12352200
NACRES:
NA.77
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Nom du produit

Protease Inhibitor Cocktail powder, for use with bacterial cell extracts, lyophilized powder

form

lyophilized powder

solubility

water: soluble

storage temp.

−20°C

Quality Level

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Application

The protease inhibitor cocktail improves the yields of intact proteins by adding inhibitors to enzymes that modify proteins present in cell extracts. This product has been optimized and tested for bacterial cell use, with broad specificity against serine, cysteine, and aspartic proteases, metalloproteases, and aminopeptidases.

Biochem/physiol Actions

This mixture contains individual components, including AEBSF at 23 mM, EDTA at 100 mM, Bestatin at 2 mM, Pepstatin A at 0.3 mM, and E-64 at 0.3 mM. AEBSF acts to inhibit serine proteases, including trypsin, chymotrypsin, and plasmin amongst others. Bestatin inhibits aminpeptidases. E-64 acts against cystein proteases. Pepstatin A inhibits acid proteases. EDTA is an inhibitor of metalloproteases.

Disclaimer

The lyophilized powder is stable for at least 2 years when stored unopened at -20°C. It is also supplied with a vial of DMSO. A prepared solution in DMSO and water will remain clear and colorless for approximately 24 hours at 4°C, before the inhibitors will precipitate out.

Features and Benefits

Broad specificity against serine, cysteine, aspartic, and metalloproteases, as well as aminopeptidases.

Contains individual components, including AEBSF, EDTA, Bestatin, Pepstatin A, and E-64, each targeting specific types of proteases.

Lyophilized powder is stable for at least 2 years when stored unopened at -20°C.

Supplied with a vial of DMSO for preparation of a cocktail solution.

One mL of the cocktail solution is recommended for the inhibition of protease activity found in 20 mL of cell lysate from 4g of E. coli cells.

General description

The Protease Inhibitor Cocktail is a lyophilized powder for use in the inhibition of proteases present in bacterial cell extracts.

The product contains individual components that target serine, cysteine, aspartic, and metalloproteases, as well as aminopeptidases.

Preparation Note

A cocktail solution may be prepared by adding 1 mL of DMSO and 4 mL of deionized water to the 5 mL size or 5 mL of DMSO and 20 mL of deionized water to the 25 mL size. One mL of the cocktail solution is recommended for the inhibition of the protease activity found in 20 mL of cell lysate from 4g of E. coli cells.

signalword

Danger

Hazard Classifications

Acute Tox. 4 Inhalation - Eye Dam. 1 - Met. Corr. 1 - Skin Corr. 1A - STOT RE 2 Inhalation

target_organs

Respiratory Tract

Classe de stockage

8A - Combustible corrosive hazardous materials

wgk

WGK 3

ppe

Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges


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Ryan W Bogard et al.
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Evgeniy V Petrotchenko et al.
Molecular & cellular proteomics : MCP, 11(7), M111-M111 (2012-03-23)
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H Cao et al.
Plant physiology, 120(1), 205-216 (1999-05-11)
This study identified the complement of soluble starch synthases (SSs) present in developing maize (Zea mays) endosperm. The product of the du1 gene, DU1, was shown to be one of the two major soluble SSs. The C-terminal 450 residues of
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Applied and environmental microbiology, 86(22) (2020-08-10)
Peptides present in growth media are essential for nitrogen nutrition and optimal growth of lactic acid bacteria. In addition, according to their amino acid composition, they can also directly or indirectly play regulatory roles and influence global metabolism. This is
Kerri Kobryn et al.
Molecular cell, 9(1), 195-201 (2002-01-24)
The genus Borrelia includes the causative agents of Lyme disease and relapsing fever. An unusual feature of these bacteria is a segmented genome consisting mostly of a number of linear DNA molecules with covalently closed hairpin ends or telomeres. In

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