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P1860

Sigma-Aldrich

Protease Inhibitor Cocktail

for use in tissue culture media, DMSO solution

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Synonym(s):
protease inhibitor
EC Number:
200-664-3
MDL number:
MFCD00677817
NACRES:
NA.77

Quality Level

200

form

DMSO solution

shipped in

dry ice

storage temp.

−20°C

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P8340P9599P8849
Protease Inhibitor Cocktail for use in tissue culture media, DMSO solution

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P1860

Protease Inhibitor Cocktail

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P8340

Protease Inhibitor Cocktail

Protease Inhibitor Cocktail for plant cell and tissue extracts, DMSO solution

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P9599

Protease Inhibitor Cocktail

Protease Inhibitor Cocktail for use in purification of Histidine-tagged proteins, DMSO solution

Sigma-Aldrich

P8849

Protease Inhibitor Cocktail

shipped in

dry ice

shipped in

-

shipped in

-

shipped in

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

300

Quality Level

300

Quality Level

300

General description

The Protease Inhibitor Cocktail is a mixture of protease inhibitors designed to prevent proteolytic degradation of secreted proteins in tissue culture media.

Specificity

Inhibits serine, cysteine, aspartic proteases, and aminopeptidases

Application

This product is specifically optimized for use in tissue culture media and can be added after 48 hours of exposure to fresh medium to ensure the continued inhibition of proteases.

Features and Benefits

Broad specificity: Inhibits serine, cysteine, aspartic proteases, and aminopeptidases

Non-toxic: After 48 hours exposure, the product is non-toxic to adherent cell lines A431, CHO, COS, HepG2 and HeLa; and to Jurkat and HL-60 cell lines grown in suspension.

Contains no metal chelators: Ensures compatibility with downstream applications

Convenient packaging: 1 mL in glass bottle

Easy to use: Use at a dilution of 1:200 or more in tissue culture media to prevent proteolytic degradation of secreted proteins.

Components

Aprotinin
Bestatin
E-64
Leupeptin
Pepstatin A

Other Notes

Mixture of protease inhibitors with broad specificity for the inhibtion of serine, cysteine, aspartic and aminopeptidases. Contains aprotinin, bestatin, leupeptin, E-64, and pepstatin A. Contains no metal chelators

Caution

After 48 hours exposure, the product is non-toxic to adherent cell lines A431, CHO, COS, HepG2 and HeLa; and to Jurkat and HL-60 cell lines grown in suspension.

Quantity

Use at a dilution of 1:200 or more in tissue culture media to prevent proteolytic degradation of secreted proteins.

Physical form

Solution in DMSO (D 2650, Hybri-Max).

related product

Product No.
Description
Pricing

P8465

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

P8340

Protease Inhibitor Cocktail, for use with mammalian cell and tissue extracts, DMSO solution

P8215

Protease Inhibitor Cocktail, for use with fungal and yeast extracts, DMSO solution

P2714

Protease Inhibitor Cocktail powder, for general use, lyophilized powder

P8849

Protease Inhibitor Cocktail, for use in purification of Histidine-tagged proteins, DMSO solution

P9599

Protease Inhibitor Cocktail, for plant cell and tissue extracts, DMSO solution

S8820

SIGMAFAST™ Protease Inhibitor Tablets, For General Use

S8830

SIGMAFAST™ Protease Inhibitor Cocktail Tablets, EDTA-Free, for use in purification of Histidine-tagged proteins

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

188.6 °F

Flash Point(C)

87 °C

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Matthew Townsend et al.
The Journal of physiology, 572(Pt 2), 477-492 (2006-02-14)
The accumulation of amyloid beta-protein (Abeta) in brain regions serving memory and cognition is a central pathogenic feature of Alzheimer's disease (AD). We have shown that small soluble oligomers of human Abeta that are naturally secreted by cultured cells inhibit
Takuma Shiratori et al.
Journal of immunology (Baltimore, Md. : 1950), 200(1), 218-228 (2017-11-17)
As osteoclasts have the central roles in normal bone remodeling, it is ideal to regulate only the osteoclasts performing pathological bone destruction without affecting normal osteoclasts. Based on a hypothesis that pathological osteoclasts form under the pathological microenvironment of the
Noëlle Dommann et al.
Cancers, 12(7) (2020-07-19)
Colorectal cancer, along with its high potential for recurrence and metastasis, is a major health burden. Uncovering proteins and pathways required for tumor cell growth is necessary for the development of novel targeted therapies. Ajuba is a member of the
Asja Guzman et al.
Biomaterials, 115, 19-29 (2016-11-24)
Invasive breast cancer and other tumors of epithelial origin must breach a layer of basement membrane (BM) that surrounds the primary tumor before invading into the adjacent extracellular matrix. To analyze invasive strategies of breast cancer cells during BM breaching
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