P8465

Sigma-Aldrich

Protease Inhibitor Cocktail powder

for use with bacterial cell extracts, lyophilized powder

NACRES:
NA.77
Pricing and availability is not currently available.

Quality Level

form

lyophilized powder

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

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.

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.

Pictograms

Corrosion

Signal Word

Danger

Hazard Statements

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Certificate of Analysis
Certificate of Origin
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...
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...
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...
Drishya Diwaker et al.
PLoS pathogens, 16(6), e1008597-e1008597 (2020-06-09)
During infection of neurons by alphaherpesviruses including Pseudorabies virus (PRV) and Herpes simplex virus type 1 (HSV-1) viral nucleocapsids assemble in the cell nucleus, become enveloped in the cell body then traffic into and down axons to nerve termini for...

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.