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S8830

Sigma-Aldrich

Protease Inhibitor Cocktail

SIGMA FAST, EDTA-Free, tablet, for the inhibition of serine, cysteine, aspartic and metalloproteases, for use in purification of Histidine-tagged proteins

Synonym(s):

Protease Inhibitor Cocktail

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About This Item

MDL number:
MFCD00677817
UNSPSC Code:
12352200
NACRES:
NA.77

product name

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

biological source

bovine lung

Quality Level

200

form

tablet

storage temp.

2-8°C

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General description

SIGMAFAST™ Protease Inhibitor Cocktail Tablets, EDTA-Free is a water-soluble tablet formulation designed to inhibit serine, cysteine, aspartic and metalloproteases. The tablets contain no strong metal chelators, such as EDTA, and are compatible with sample processing by immobilized metal affinity chromatography (IMAC). The tablets also contain a unique, proprietary formulation that includes a pepstatin A salt for additional protection.

Specificity

Inhibits serine, cysteine, aspartic, and metalloproteases.

Application

The broad specificity of SIGMAFAST™ Protease Inhibitor Cocktail Tablets makes them suitable for use in the purification of histidine-tagged proteins and as a general-purpose protease inhibitor cocktail. The tablets can also be used as components of buffers for cell lysis, and have been optimized and tested for use with HIS-Select media.

Features and Benefits

EDTA-Free: Contains no strong metal chelators, such as EDTA, which might interfere with IMAC processing.

Pepstatin A: Contains a unique, proprietary formulation that includes a pepstatin A salt for additional protection not normally obtained in a tablet format.

Broad Specificity: Inhibits serine, cysteine, aspartic, and metalloproteases, providing broad protection for protein samples.

High Yield: One tablet makes 100 mL of cocktail, and is recommended for the inhibition of the proteases present in a maximum of 20 g of cell mass in 100 mL of extract.

Long Stability: The tablets are stable as supplied for at least 2 years at 2–8 °C, and the reconstituted protease inhibitor solution (1´ or 10´) is stable for at least 2 weeks at 2–8 °C.

Components

AEBSF
Bestatin
E-64
Pepstatin A
Phosphoramidon
Leupeptin
Aprotinin

Quantity

One tablet makes 100 mL of cocktail. One tablet is recommended for the inhibition of the proteases present in a maximum of 20 g of cell mass in 100 mL of extract.

Physical form

Tablet that is water soluble

Storage and Stability

The tablets are stable as supplied for at least 2 years at 2–8 °C. The reconstituted protease inhibitor solution (1´ or 10´) is stable for at least 2 weeks at 2–8 °C.

Legal Information

SIGMAFAST is a trademark of Sigma-Aldrich Co. LLC

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pictograms

Corrosion
GHS05

signalword

Danger

hcodes

H314

Hazard Classifications

Eye Dam. 1 - Skin Corr. 1A

Storage Class

8A - Combustible corrosive hazardous materials

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges

Certificates of Analysis (COA)

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Stephan G Mauracher et al.
Phytochemistry, 99, 14-25 (2014-01-28)
Tyrosinases catalyze two initial reaction steps in the formation of melanin. Purification of tyrosinases had always been a process accompanied with various problems caused by enzymatic browning processes. Here, an approach is presented for the purification of the latent enzyme
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BMC genomics, 13, 380-380 (2012-08-10)
Filamentous fungi are confronted with changes and limitations of their carbon source during growth in their natural habitats and during industrial applications. To survive life-threatening starvation conditions, carbon from endogenous resources becomes mobilized to fuel maintenance and self-propagation. Key to
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Jeffrey L Waugh et al.
PloS one, 6(11), e27984-e27984 (2011-12-02)
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Journal of neurochemistry, 120(1), 56-69 (2011-11-01)
Detergent-resistant membranes (DRM) are thought to contain structures such as lipid rafts that are involved in compartmentalizing cell membranes. We report that the majority of D(2)-dopamine receptors (D(2)R) expressed endogenously in mouse striatum or expressed in immortalized cell-lines is found
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Aprotinin

While aprotinin and bovine pancreatic trypsin inhibitor (BPTI) are the same protein sequence, the term aprotinin is typically used when describing the protein derived from bovine lung.

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