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Protein Phosphatase 2A C subunit (human recombinant; L309 deletion)

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    Protein Phosphatase 2A C subunit (human recombinant; L309 deletion)
  • Protein Phosphatase 2A C subunit (human recombinant; L309 deletion)
Cat No: 10011237
Proteins - Enzymes
Cayman
€310.00
Price is excluding VAT and does not include packaging neither shipping

Reversible protein phosphorylation is a fundamental regulatory mechanism in all aspects of biology. Protein phosphatase 2A (PP2A) is a divalent cation-independent protein serine/threonine phosphatase involved in regulating numerous cellular processes ...

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: 10 µg

This product can only be bought through Cayman Chemical. Please contact us.

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Territorial Availability: Available through Bertin Technologies only in Europe
Correlated keywords:
  • protein phosphatase 2A PP-2A PP2A serine threonine enzyme kinetic regulation dephosphorylate substrate
Product Overview:
Reversible protein phosphorylation is a fundamental regulatory mechanism in all aspects of biology. Protein phosphatase 2A (PP2A) is a divalent cation-independent protein serine/threonine phosphatase involved in regulating numerous cellular processes including the cell cycle, growth and differentiation and is also thought to be a potential tumor suppressor.{15392} PP2A is a hetrotrimeric protein containing a 65 kDa scaffolding A subunit, a regulatory B subunit and a 36 kDa catalytic C subunit.{15393} The recombinant PP2A catalytic subunit has the characteristic properties of Type 2A phosphatases and is highly sensitive to okadaic acid and microcystins.{15391} The provided preparation of the catalytic subunit of PP2A is useful for the study of enzyme kinetics and regulation, to dephosphorylate target substrates and to evaluate the effects of test substances on the activity of the phosphatase.
Size 10 µg
Shipping dry ice
Stability Store at -80 degrees; shelf life 365 days
Formulation 20 mM Tris, pH 7.5, 100 mM sodium chloride, 5 mM MgCl2, 1 mM EDTA, and 25% glycerol
Custom Code 3507.90
UNSPSC code 12352204

Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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