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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

Código UNSPSC:
12352200
NACRES:
NA.77
Formulario:
lyophilized powder
temp. de almacenamiento:
−20°C

Nombre del producto

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

Nivel de calidad

300

Formulario

lyophilized powder

temp. de almacenamiento

−20°C

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Categorías relacionadas

Descripción general

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.

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Características y beneficios

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.

Precaución

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.

Nota de preparación

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.

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Palabra de señalización

Danger

Frases de peligro

H290,H314,H332,H373

Clasificaciones de peligro

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

Órganos de actuación

Respiratory Tract

Código de clase de almacenamiento

8A - Combustible corrosive hazardous materials

Clase de riesgo para el agua (WGK)

WGK 3

Equipo de protección personal

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

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Certificados de análisis (COA)

Lot/Batch Number
0000355404
0000303638
0000355404
0000303638
0000213110

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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
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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
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Applied and environmental microbiology, 86(22) (2020-08-10)
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H Cao et al.
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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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Contenido relacionado

Protease Inhibitor Selection: Avoid Protein Loss 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.

Protease Inhibitor Selection: Avoid Protein Loss 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.

Protease Inhibitor Selection: Avoid Protein Loss 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.

Protease Inhibitor Selection: Avoid Protein Loss 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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