539137
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
Form:
lyophilized
Solubility:
water: soluble
Storage temp.:
−20°C
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)
solubility
water: soluble
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. 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
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)
Signal Word
Danger
Hazard Statements
Precautionary 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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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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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.
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
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
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