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Merck

539137

Protease Inhibitor Cocktail V

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

Synonyme(s) :

EDTA free Protease inhibitor

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A propos de cet article

UNSPSC Code:
12352200
NACRES:
NA.54
Form:
lyophilized
Solubility:
water: soluble
Storage temp.:
−20°C

Principaux documents

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Nom du produit

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

form

lyophilized

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze, desiccated (hygroscopic)

solubility

water: soluble

shipped in

wet ice

storage temp.

−20°C

Quality Level

100

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Catégories apparentées

General description

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.

Biochem/physiol Actions

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

Preparation Note

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

Disclaimer

Toxicity: Standard Handling (A)

hcodes

H314

pictograms

Corrosion
GHS05

signalword

Danger

Hazard Classifications

Eye Dam. 1 - Skin Corr. 1A

Classe de stockage

8A - Combustible corrosive hazardous materials

wgk

WGK 3

Certificats d'analyse (COA)

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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
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
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
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
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
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