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USP2 active domain (human recombinant)

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    USP2 active domain (human recombinant)
  • USP2 active domain (human recombinant)
Cat No: 22784
Proteins - Enzymes
Cayman

Ubiquitin-specific protease 2 (USP2), also known as ubiquitin carboxyl-terminal hydrolase 2, is a cysteine protease involved in intracellular protein degradation by deubiquitinating degraded protein, including Mdm2, Mdm4, and CCND1.{40253,40254,40255}...

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: 100 µg

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Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • USP-2 UBP41 UBP-41 USP9 protease MDM-2 4 CCND-1 PER-1 9 Escherichia deubiquitinating enzyme carboxyl-terminal thioesterase FAS
Product Overview:
Ubiquitin-specific protease 2 (USP2), also known as ubiquitin carboxyl-terminal hydrolase 2, is a cysteine protease involved in intracellular protein degradation by deubiquitinating degraded protein, including Mdm2, Mdm4, and CCND1.{40253,40254,40255} In both normal and cancer cells, it regulates G1/S cell-cycle transition.{40254} It may regulate p53-dependent pathways by deubiquitinating Mdm2, indirectly promoting p53 degradation and limiting its activity.{40253,40256,40257}. Regulated by androgen, USP2 is over-expressed in prostate cancer and stabilizes fatty acid synthase (FASN), which is associated with the malignancy of some aggressive prostate cancers.{40256,40258} Some of these oncogenic properties may be linked to its deubiquitinating activity. One hypothesis is that USP2 may stabilize short-lived proteins that may act to induce apoptosis.{40259} USP2 has also been shown to regulate the intrinsic circadian rhythm and its capacity to respond to external cues, in a non-degradative manner by acting on the core clock component PER1.{40260} This protein is a truncation containing the active catalytic domain (residues 259-605) of USP2 and a C-terminal His-tag.
Size 100 µg
Shipping dry ice
Formulation 50 mM HEPES, pH 8.0, 150 mM sodium chloride, 1 mM DTT, and 0.1 mM EDTA
Purity ≥95% estimated by SDS-PAGE
Custom Code 3507.90
UNSPSC code 12352204

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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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