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539137

Sigma-Aldrich

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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About This Item

Code UNSPSC :
12352200
Nomenclature 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.

Niveau de qualité

Forme

lyophilized

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
desiccated (hygroscopic)

Conditions d'expédition

wet ice

Température de stockage

−20°C

Description générale

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.

Spécificité

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

Actions biochimiques/physiologiques

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

Avertissement

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.

Informations légales

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

Pictogrammes

Corrosion

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Dam. 1 - Skin Corr. 1A

Code de la classe de stockage

8A - Combustible corrosive hazardous materials

Classe de danger pour l'eau (WGK)

WGK 3


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Consulter la Bibliothèque de documents

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
Jennyfer Tena et al.
Molecular & cellular proteomics : MCP, 21(11), 100427-100427 (2022-10-18)
The proteins in the cell membrane of the brain are modified by glycans in highly interactive regions. The glycans and glycoproteins are involved in cell-cell interactions that are of fundamental importance to the brain. In this study, the comprehensive N-glycome
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

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