Halt™ Protease Inhibitor Cocktail, EDTA-Free (100X)
Halt™ Protease Inhibitor Cocktail, EDTA-Free (100X)
Thermo Scientific™

Halt™ Protease Inhibitor Cocktail, EDTA-Free (100X)

Thermo Scientific Halt Protease Inhibitor Cocktail, EDTA-free (100X) are ready-to-use concentrated stock solutions of protease inhibitors for addition to samplesRead more
Catalog NumberQuantity
7842524 x 100 μL
784375 mL
7843910 mL
877851 mL
Catalog number 78425
Price (JPY)
50,800
Each
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Quantity:
24 x 100 μL
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Thermo Scientific Halt Protease Inhibitor Cocktail, EDTA-free (100X) are ready-to-use concentrated stock solutions of protease inhibitors for addition to samples to prevent proteolytic degradation during cell lysis and protein extraction.

Features of Halt Protease Inhibitor Cocktail, EDTA-free (100X):

Convenient—the refrigerator-stable, 100X liquid format is more effective and easier to use than individual inhibitors or other formats; just pipette exactly the amount you need
No proprietary ingredients—fully disclosed formulation contains optimized concentrations of six broad-spectrum protease inhibitors AEBSF, aprotinin, bestatin, E-64, leupeptin and pepstatin A stabilized in high-quality dimethylsulfoxide (DMSO)
Multiple package sizes—choose among several package sizes, including single-use microtubes that keep protease inhibitors fresh and reduce the risk of reagent contamination
EDTA-free formulations—ensures compatibility with isoelectric focusing
Lysis buffer compatible—use with Thermo Scientific Pierce Cell Lysis Buffers or nearly any other commercial or homemade detergent-based lysis reagent. Add 10 μL of concentrated cocktail per 1 mL of lysis buffer to ensure complete protection of the resulting protein extract.

Applications:
• Protection of intact, active cellular proteins from degradation by endogenous proteases
• Inhibition of protease activity from lysates produced by a variety of methods including Thermo Scientific Pierce Cell Lysis Reagents, other commercially formulated cell or tissue lysis products, sonication, French press, blender homogenization or repetitive freeze/thaw cycling
• Screening of extracts for proteolytic activity
• The study of proteolysis in the regulation of cellular processes

Proteases make up a large category of enzymes, including endopeptidases and exopeptidases, which catalyze the hydrolytic breakdown of proteins into peptides or amino acids in a wide variety of cell and tissue types. Proteases are regulated and compartmentalized in living cells, but cell lysis releases and mixes them with other extracted proteins. Their activity can thus lead to the loss of a large number of valuable proteins, adversely affecting downstream applications. For this reason, it is common practice to spike cell lysis buffers or cell extracts with a cocktails of compounds known to inactivate or inhibit proteases. Halt Protease Inhibitor Cocktails effectively inhibit serine-proteases, cysteine-proteases, aspartic acid-proteases and aminopeptidases that are typically present in cellular lysate samples. Regular and EDTA-free formulations provide for inhibition of metalloproteases and compatibility with 2D electrophoresis, respectively.

Related Products
Halt™ Protease Inhibitor Single-Use Cocktail (100X)
For Research Use Only. Not for use in diagnostic procedures.
Specifications
BufferLysis Buffer
InhibitorsProtease Inhibitor
Quantity24 x 100 μL
Reagent TypeProtease Inhibitor
FormLiquid
Product LineHalt™
Product TypeProtease Inhibitor Cocktail
Unit SizeEach
Contents & Storage
Upon receipt store at 4°C
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Frequently asked questions (FAQs)

What are the compositions of the Halt Protease Inhibitor Cocktail, EDTA-Free (100X) (Cat. No. 87785) and Halt Protease Inhibitor Cocktail (100X) (Cat. No. 87786)?

Both formulations are the same and have the following composition:

What is the shelf life of Halt Protease Inhibitor Cocktail, EDTA-free (100X) (Cat. No. 78425)?

The Halt Protease Inhibitor Cocktail, EDTA-free (100X) (Cat. No. 78425) is covered under our general 1-year warranty and is guaranteed to be fully functional for 12 months from the date of shipment, if stored as recommended. Please see section 8.1 of our Terms & Conditions of Sale for more details.

Can I use just part of the Pierce Protease Inhibitor XL Capsules, EDTA-Free and save part of the capsule for later use?

We do not recommend “splitting” the capsule into smaller portions. Researchers using less than 500 mL should choose a different format (liquid or tablet) of protease inhibitors.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

What formats of protease inhibitors do you offer?

We offer standalone protease inhibitors (AEBSF, Aprotinin, PMSF, EDTA, etc.), as well as cocktails or combinations of protease inhibitors in liquid, tablet, and larger capsule formats. These cocktails of protease inhibitors can also be purchased in combination with a cocktail of phosphatase inhibitors, in both liquid and tablet form, for even greater convenience.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

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Certificates

Lot #Certificate TypeDateCatalog Number(s)
3214421Certificate of AnalysisJul 03, 202578425
3215046Certificate of AnalysisJun 17, 202587785
3215610Certificate of AnalysisJun 17, 202587785
3215043Certificate of AnalysisJun 17, 202578439
3214005Certificate of AnalysisJun 11, 202587785
5 results displayed, search above for a specific certificate

Safety Data Sheets

Citations & References (5)

Citations & References
Abstract
Dietary and water restriction leads to increased susceptibility to antimicrobial resistant pathogens.
Authors:Lacey KA,Pickrum AM,Gonzalez S,Bartnicki E,Castellaw AH,Rodrick TC,Jones DR,Khanna KM,Torres VJ
Journal:Science advances
PubMed ID:39047095
Dehydration and malnutrition are common and often underdiagnosed in hospital settings. Multidrug-resistant bacterial infections result in more than 35,000 deaths a year in nosocomial patients. The effect of temporal dietary and water restriction (DWR) on susceptibility to multidrug-resistant pathogens is unknown. We report that DWR markedly increased susceptibility to systemic ... More
Cooperation between the Hippo and MAPK pathway activation drives acquired resistance to TEAD inhibition.
Authors:Paul S,Hagenbeek TJ,Tremblay J,Kameswaran V,Ong C,Liu C,Guarnaccia AD,Mondo JA,Hsu PL,Kljavin NM,Czech B,Smola J,Nguyen DAH,Lacap JA,Pham TH,Liang Y,Blake RA,Gerosa L,Grimmer M,Xie S,Daniel B,Yao X,Dey A
Journal:Nature communications
PubMed ID:39966375
TEAD (transcriptional enhanced associate domain) transcription factors (TEAD1-4) serve as the primary effectors of the Hippo signaling pathway in various cancers. Targeted therapy leads to the emergence of resistance and the underlying mechanism of resistance to TEAD inhibition in cancers is less characterized. We uncover that upregulation of the AP-1 ... More
FOXO1 modulates osteoblast differentiation.
Authors:Siqueira MF,Flowers S,Bhattacharya R,Faibish D,Behl Y,Kotton DN,Gerstenfeld L,Moran E,Graves DT
Journal:Bone
PubMed ID:21281751
Forkhead box O1 (FOXO1) is upregulated during bone formation and in response to stimulation by bone morphogenetic proteins. Studies presented here examined the functional role of FOXO1 in a well defined culture system in which pre-osteoblastic cells undergo terminal differentiation in vitro. Mineralizing cultures of MC3T3-E1 cells were examined with ... More
miR-34c is downregulated in prostate cancer and exerts tumor suppressive functions.
Authors:Hagman Z, Larne O, Edsjö A, Bjartell A, Ehrnström RA, Ulmert D, Lilja H, Ceder Y
Journal:Int J Cancer
PubMed ID:21351256
MicroRNAs (miRNAs) are small noncoding RNAs that post-transcriptionally regulate gene expression. There have been several reports of miRNA deregulation in prostate cancer (PCa) and the biological evidence for an involvement of miRNAs in prostate tumorigenesis is increasing. In this study, we show that miR-34c is downregulated in PCa (p = ... More
Glucagon-like peptide 1 inhibits cell apoptosis and improves glucose responsiveness of freshly isolated human islets.
Authors:Farilla L, Bulotta A, Hirshberg B, Li Calzi S, Khoury N, Noushmehr H, Bertolotto C, Di Mario U, Harlan DM, Perfetti R
Journal:Endocrinology
PubMed ID:12960095
The peptide hormone, glucagon-like peptide 1 (GLP-1), has been shown to increase glucose-dependent insulin secretion, enhance insulin gene transcription, expand islet cell mass, and inhibit beta-cell apoptosis in animal models of diabetes. The aim of the present study was to evaluate whether GLP-1 could improve function and inhibit apoptosis in ... More
5 total citations

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