Description
Key facts
Purity:>95% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:400,000 U/mg. 400 U/μl, where one unit is defined as the amount of enzyme that hydrolyzes 1 nmole of p-nitrophenyl phosphate per minute at 30°C. Unit definition assays are performed with 50mM p-nitrophenyl phosphate in λ-PPase buffer, supplemented with 2 mM MnCl2 in a 50 μl reaction.,
Accession:P03772,
Animal free:No,
Carrier free:No,
Species:Bacteriophage lambda,
Storage buffer:pH: 6 - 8.5Constituents: 50% Glycerol (glycerin, glycerine), 1.19% HEPES, 0.58% Sodium chloride, 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.01% Polyoxyethylene lauryl ether, 0.002% EDTA, 0.001% Manganese chloride
Product details:
ab188459 can be used to release phosphate groups from phosphorylated serine, threonine, tyrosine and histidine residues in proteins
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Serine/threonine-protein phosphatase is an enzyme that reverses phosphorylation of serine and threonine residues in various proteins. Popular alternate names include protein phosphatase lambda protein phosphatase and phosphatase protein. The enzyme is found in many tissues with high expression in the brain liver and muscle tissues. Its mass is approximately 35 kilodaltons. The enzyme acts by dephosphorylating target proteins countering the action of kinases. This process plays a central role in the regulation of cellular functions through modification of protein activity location and interactions.
Biological function summary
Serine/threonine-protein phosphatases participate in cell cycle control apoptosis metabolism and cellular stress responses. These phosphatases often form part of larger protein complexes to achieve specificity and efficient catalytic activity. They regulate the phosphorylation state of key signaling molecules which affects their function. This regulation ensures proper signal transduction impacting various cellular decisions and responses to environmental cues. The phosphatase activity is tightly controlled by regulatory proteins and cellular signals to maintain balance in cellular signaling pathways.
Pathways
Serine/threonine-protein phosphatases play a significant role in the MAPK/ERK and mTOR signaling pathways. Inhibition or activation by these phosphatases modulates the response to growth factors and nutrient availability impacting cell growth proliferation and survival. They work with proteins such as MAP kinases and PI3-kinase to finely tune cellular responses. These interactions highlight the enzyme's involvement in translating external signals into appropriate cellular responses which is important for maintaining cellular homeostasis and function.
Altered activity of serine/threonine-protein phosphatases associates with cancer and neurodegenerative diseases. Aberrant phosphatase function can disrupt cell cycle control leading to uncontrolled cell proliferation in cancers such as colon or breast cancer. In neurodegenerative diseases like Alzheimer's changes in phosphorylation states of tau protein mediated by phosphatases contribute to disease progression. These connections implicate regulatory and structural proteins like tau and cyclin-dependent kinases emphasizing the importance of balanced phosphatase activity in health and disease.
