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Sigma-Aldrich

Protease Inhibitor Cocktail V

EDTA-Free, lyophilized, A cocktail of four protease inhibitors for the inhibition of serine, cysteine, but not metalloproteases.

Synonym(s):

EDTA free Protease inhibitor

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.54

product name

Protease Inhibitor Cocktail Set V, EDTA-Free, A cocktail of four protease inhibitors for the inhibition of serine, cysteine, but not metalloproteases.

Quality Level

form

lyophilized

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)

shipped in

wet ice

storage temp.

−20°C

General description

A cocktail of four protease inhibitors for the inhibition of serine, cysteine, but not metalloproteases. Recommended for use with mammalian cell lysates and tissue extracts. Provided as a single vial or a set of 10 vials. When reconstituted each vial contains a 100X stock solutions. When diluted to 1X the cocktail contains the following components:
A cocktail of four protease inhibitors for the inhibition of serine, cysteine, but not metalloproteases. Reconstitute each vial with 1 ml H2O to obtain a 100X stock solution. 1X stock solution contains 500 µM AEBSF, HCl (Cat. No. 101500), 150 nM Aprotinin (Cat. No. 616370), 1 µM E-64 (Cat. No. 324890), and 1 µM Leupeptin Hemisulfate (Cat. No. 108975). Supplied with a data sheet.

Specificity

Inhibits serine proteases, cysteine proteases. Does not inhibit metalloproteases.

Biochem/physiol Actions

Cell permeable: no
Primary Target
Serine and cysteine proteases, but not metalloproteases
Product does not compete with ATP.
Reversible: no

Warning

Toxicity: Standard Handling (A)

Reconstitution

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Reconstitute each vial with 1 ml H₂O to obtain a 100X stock solution.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictograms

Corrosion

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Dam. 1 - Skin Corr. 1A

Storage Class Code

8A - Combustible corrosive hazardous materials

WGK

WGK 3


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Emery T Usher et al.
The Journal of biological chemistry, 296, 100693-100693 (2021-04-25)
Speckle-type POZ protein (SPOP) is a ubiquitin ligase adaptor that binds substrate proteins and facilitates their proteasomal degradation. Most SPOP substrates present multiple SPOP-binding (SB) motifs and undergo liquid-liquid phase separation with SPOP. Pancreatic and duodenal homeobox 1 (Pdx1), an
Jin Wen et al.
Bioorganic & medicinal chemistry, 28(20), 115711-115711 (2020-10-18)
Cyclic peptides are capable of binding to challenging targets (e.g., proteins involved in protein-protein interactions) with high affinity and specificity, but generally cannot gain access to intracellular targets because of poor membrane permeability. In this work, we discovered a conformationally
Kirby Martinez-Fonts et al.
Nature communications, 11(1), 477-477 (2020-01-26)
Proteins are targeted to the proteasome by the attachment of ubiquitin chains, which are markedly varied in structure. Three proteasome subunits-Rpn10, Rpn13, and Rpn1-can recognize ubiquitin chains. Here we report that proteins with single chains of K48-linked ubiquitin are targeted
Mario Lebendiker et al.
Methods in molecular biology (Clifton, N.J.), 1485, 257-273 (2016-10-13)
Maltose-Binding Protein (MBP) is one of the most popular fusion partners being used for producing recombinant proteins in bacterial cells. MBP allows the use of a simple capture affinity step on Amylose-Agarose or Dextrin-Sepharose columns, resulting in a protein that
Emery T Usher et al.
Biophysical journal, 120(21), 4710-4721 (2021-10-01)
Post-translational modification (PTM) of proteins is of critical importance to the regulation of many cellular processes in eukaryotic organisms. One of the most well-studied protein PTMs is methylation, wherein an enzyme catalyzes the transfer of a methyl group from a

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