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Merck

P8465

Sigma-Aldrich

Protease Inhibitor Cocktail

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

Sinónimos:

Protease inhibitor

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.77

product name

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

Quality Level

form

lyophilized powder

storage temp.

−20°C

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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.

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.

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.

Caution

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.

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

Storage Class

8A - Combustible corrosive hazardous materials

wgk_germany

WGK 3

ppe

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


Certificados de análisis (COA)

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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
Ryan W Bogard et al.
mBio, 3(5), e00236-e00212 (2012-09-28)
LysR-type transcriptional regulators (LTTRs) are the largest, most diverse family of prokaryotic transcription factors, with regulatory roles spanning metabolism, cell growth and division, and pathogenesis. Using a sequence-defined transposon mutant library, we screened a panel of V. cholerae El Tor
Evgeniy V Petrotchenko et al.
Molecular & cellular proteomics : MCP, 11(7), M111-M111 (2012-03-23)
Chemical cross-linking combined with mass spectrometry is a rapidly developing technique for structural proteomics. Cross-linked proteins are usually digested with trypsin to generate cross-linked peptides, which are then analyzed by mass spectrometry. The most informative cross-links, the interpeptide cross-links, are
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
Lucas Proust et al.
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

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Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.

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