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Citations & References (6)
Thermo Scientific™
Halt™ Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X)
Thermo Scientific Halt Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X) provides the convenience of a single solution with full proteinRead more
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| Catalog Number | Quantity |
|---|---|
| 78447 | 10 mL |
| 78441 | 1 mL |
| 78443 | 24 x 100 μL |
| 78445 | 5 x 1 mL |
Catalog number 78447
Price (TWD)
47,550.00
온라인 행사
Ends: 31-Dec-2025
63,400.00Save 15,850.00 (25%)
Each
Quantity:
10 mL
Price (TWD)
47,550.00
온라인 행사
Ends: 31-Dec-2025
63,400.00Save 15,850.00 (25%)
Each
Thermo Scientific Halt Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X) provides the convenience of a single solution with full protein sample protection for cell and tissue lysates.
Features of Halt Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X):
• Complete protection—all-in-one cocktail contains both protease and phosphatase inhibitors
• Multiple package sizes—choose from four convenient packages sizes to match nearly any scale
• Convenient —the 100X liquid formulation is much easier and more effective to use than individual inhibitors and other formats
• Easy storage—aqueous-based format allows for convenient cold-room storage without freezing, by contrast with DMSO-based cocktails
• Compatible—can be used in mass spectrometry (MS) because it does not contain AEBSF, which can cause peaks to shift
• Validated—fully compatible with Thermo Scientific Pierce Cell Lysis Buffers
Halt Protease and Phosphatase Inhibitor Cocktail is specifically optimized to protect proteins from degradation during extraction and purification. The cocktail contains inhibitors against the major classes of proteases and phosphatases, targeting aminopeptidases, cysteine and serine proteases and serine/threonine and protein tyrosine phosphatases.
Related Products
Halt™ Protease and Phosphatase Inhibitor Cocktail (100X)
Features of Halt Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X):
• Complete protection—all-in-one cocktail contains both protease and phosphatase inhibitors
• Multiple package sizes—choose from four convenient packages sizes to match nearly any scale
• Convenient —the 100X liquid formulation is much easier and more effective to use than individual inhibitors and other formats
• Easy storage—aqueous-based format allows for convenient cold-room storage without freezing, by contrast with DMSO-based cocktails
• Compatible—can be used in mass spectrometry (MS) because it does not contain AEBSF, which can cause peaks to shift
• Validated—fully compatible with Thermo Scientific Pierce Cell Lysis Buffers
Halt Protease and Phosphatase Inhibitor Cocktail is specifically optimized to protect proteins from degradation during extraction and purification. The cocktail contains inhibitors against the major classes of proteases and phosphatases, targeting aminopeptidases, cysteine and serine proteases and serine/threonine and protein tyrosine phosphatases.
Related Products
Halt™ Protease and Phosphatase Inhibitor Cocktail (100X)
For Research Use Only. Not for use in diagnostic procedures.
Specifications
BufferLysis Buffer
DescriptionHalt Protease and Phosphatase Inhibitor Cocktail, EDTA-Free
InhibitorsProtease Inhibitor, Phosphatase Inhibitor
Quantity10 mL
Reagent TypeProtease Inhibitor, Phosphatase Inhibitor
FormLiquid
Product LineHalt
Product TypeProtease and Phosphatase Inhibitor Cocktail
Unit SizeEach
Contents & Storage
Upon receipt store at 4°C. Product shipped with an ice pack. Do not freeze product.
Frequently asked questions (FAQs)
Can I store the 1X solution of the Halt Protease and Phosphatase Inhbitor Cocktail and if so, for how long?
What are the concentrations of the various components of the combined Halt Protease and Phosphatase Inhibitor Cocktail?
Do you offer the components of the Halt Protease and Phosphatase Cocktail individually?
When do I need to add EDTA when using the Halt Protease and Phosphatase Cocktail?
How much of the Halt Protease and Phosphatase Cocktail do I use for my sample?
Citations & References (6)
Citations & References
Abstract
2-Aminopyridine-Based Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 (MAP4K4) Inhibitors: Assessment of Mechanism-Based Safety.
Journal:Journal of medicinal chemistry
PubMed ID:29570292
Studies have linked the serine-threonine kinase MAP4K4 to the regulation of a number of biological processes and/or diseases, including diabetes, cancer, inflammation, and angiogenesis. With a majority of the members of our lead series (e.g., 1) suffering from time-dependent inhibition (TDI) of CYP3A4, we sought design avenues that would eliminate
Deficiency of endothelial sirtuin1 in mice stimulates skeletal muscle insulin sensitivity by modifying the secretome.
Journal:Nature communications
PubMed ID:37696839
Downregulation of endothelial Sirtuin1 (Sirt1) in insulin resistant states contributes to vascular dysfunction. Furthermore, Sirt1 deficiency in skeletal myocytes promotes insulin resistance. Here, we show that deletion of endothelial Sirt1, while impairing endothelial function, paradoxically improves skeletal muscle insulin sensitivity. Compared to wild-type mice, male mice lacking endothelial Sirt1 (E-Sirt1-KO)
Mito-Mendelian interactions alter in vivo glucose metabolism and insulin sensitivity in healthy mice.
Journal:American journal of physiology. Endocrinology and metabolism
PubMed ID:34370595
The regulation of euglycemia is essential for human health with both chronic hypoglycemia and hyperglycemia having detrimental effects. It is well documented that the incidence of type 2 diabetes increases with age and exhibits racial disparity. Interestingly, mitochondrial DNA (mtDNA) damage also accumulates with age and its sequence varies with
Deciphering the interactome of Ataxin-2 and TDP-43 in iPSC-derived neurons for potential ALS targets.
Journal:PloS one
PubMed ID:39739690
Ataxin-2 is a protein containing a polyQ extension and intermediate length of polyQ extensions increases the risk of Amyotrophic Lateral Sclerosis (ALS). Down-regulation of Ataxin-2 has been shown to mitigate TDP-43 proteinopathy in ALS models. To identify alternative therapeutic targets that can mitigate TDP-43 toxicity, we examined the interaction between
Quantitative PCR analysis of DNA, RNAs, and proteins in the same single cell.
Journal:Clin Chem
PubMed ID:23014600
The single cell represents the basic unit of all organisms. Most investigations have been performed on large cell populations, but understanding cell dynamics and heterogeneity requires single-cell analysis. Current methods for single-cell analysis generally can detect only one class of analytes.