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Citações e referências (7)
Thermo Scientific™
Halt™ Protease and Phosphatase Inhibitor Cocktail (100X)
Thermo Scientific Halt Protease and Phosphatase Inhibitor Cocktail (100X) provides the convenience of a single solution with full protein sampleLeia mais
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| Número do catálogo | Quantity |
|---|---|
| 78444 | 5 x 1 mL |
| 78442 | 24 x 100 μL |
| 78446 | 10 mL |
| 78440 | 1 mL |
Número do catálogo 78444
Preço (BRL)
-
Quantity:
5 x 1 mL
Thermo Scientific Halt Protease and Phosphatase Inhibitor Cocktail (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 (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. To promote the inhibition of metalloproteases, 0.5M EDTA is provided in a separate tube.
Related Products
Halt™ Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X)
Features of Halt Protease and Phosphatase Inhibitor Cocktail (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. To promote the inhibition of metalloproteases, 0.5M EDTA is provided in a separate tube.
Related Products
Halt™ Protease and Phosphatase Inhibitor Cocktail, EDTA-free (100X)
For Research Use Only. Not for use in diagnostic procedures.
Especificações
BufferLysis Buffer
InhibitorsProtease Inhibitor, Phosphatase Inhibitor
Quantity5 x 1 mL
Reagent TypeProtease Inhibitor, Phosphatase Inhibitor
FormLiquid
Product LineHalt
Product TypeProtease and Phosphatase Inhibitor Cocktail
Unit SizeEach
Conteúdo e armazenamento
Upon receipt store at 4°C
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?
Citações e referências (7)
Citações e referências
Abstract
Host E3 ubiquitin ligase ITCH mediates Toxoplasma gondii effector GRA35-triggered NLRP1 inflammasome activation and cell-autonomous immunity.
Journal:mBio
PubMed ID:38376248
Toxoplasma gondii is an intracellular parasite that can activate the NLRP1 inflammasome leading to macrophage pyroptosis in Lewis rats, but the underlying mechanism is not well understood. In this study, we performed a genome-wide CRISPR screen and identified the dense granule proteins GRA35, GRA42, and GRA43 as the Toxoplasma effectors
LARP1 binds ribosomes and TOP mRNAs in repressed complexes.
Journal:The EMBO journal
PubMed ID:39533057
Terminal oligopyrimidine motif-containing mRNAs (TOPs) encode all ribosomal proteins in mammals and are regulated to tune ribosome synthesis to cell state. Previous studies have implicated LARP1 in 40S- or 80S-ribosome complexes that are thought to repress and stabilize TOPs. However, a molecular understanding of how LARP1 and TOPs interact with
A KIF1C-CNBP motor-adaptor complex for trafficking mRNAs to cell protrusions.
Journal:Cell reports
PubMed ID:39982819
mRNA localization to subcellular compartments is a widely used mechanism that functionally contributes to numerous processes. mRNA targeting can be achieved upon recognition of RNA cargo by molecular motors. However, our molecular understanding of how this is accomplished is limited, especially in higher organisms. We focus on a pathway that
hCLCA1 and mCLCA3 are secreted non-integral membrane proteins and therefore are not ion channels.
Journal:J Biol Chem
PubMed ID:15919655
'Proteins of the CLCA gene family have been proposed to mediate calcium-activated chloride currents. In this study, we used detailed bioinformatics analysis and found that no transmembrane domains are predicted in hCLCA1 or mCLCA3 (Gob-5). Further analysis suggested that they are globular proteins containing domains that are likely to be
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.