Phosphatase Inhibitor Cocktail (2 Tubes, 100X)

For Phosphorylation Protection, more inhibitors mean better results. So we provide Two Tubes with 8 inhibitors.

In Stock

Background & Details

Protein phosphorylation is a crucial reversible posttranslational modification that alters protein shape, impacting their activity, localization, and interaction with other molecules. A significant proportion of cellular proteins, possibly around 30%, undergo phosphorylation.

In cells, the levels of proteins are kept constant due to a balance between their synthesis and breakdown, especially when environmental conditions do not fluctuate. However, crude cellular extracts are rich in native enzymes like phosphatases and proteases, which can degrade proteins or modify them, including the removal of phosphate groups. To circumvent this, one effective strategy is the application of specific inhibitors that target these degradative enzymes.

The efficacy of preserving phosphorylation states of proteins is proportional to the effectiveness of the inhibitors used. Our products include two distinct types of inhibitor solutions, each designed to robustly block phosphatase activity, thereby ensuring more complete preservation of your protein samples' phosphorylated forms.

Components

Tube # Ingredient 100x Conc. Target
A (Aqueous) Sodium Fluoride 100 mM Acid phosphatases
Sodium Orthovanadate 100 mM Alkaline phosphatases, PTPs, ATPases
Sodium Tartrate 400 mM Acid phosphatases
Sodium Molybdate 115 mM Acid and phosphoprotein phosphatases
Imidazole 200 mM Alkaline phosphatases
B (DMSO) (-)-p-Bromotetramisole oxalate 2.5 mM Alkaline phosphatases
Cantharidin 500 μM Ser/Thr phosphatases
Microcystin LR, Microcystis aeruginosa 500 nM PP1 and PP2A

Scroll sideways to see all columns.

Specifications

Manufacturer Adooq Bioscience
Applications

Phosphatase Inhibitor Cocktail

Storage

Store at -20°C, stable storage for more than 12 months. When store at 2-8°C, the product will be stable for 2 months.

Added to your cart

View Cart Checkout
Loading...