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N-Oxalylglycine

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    N-<wbr/>Oxalylglycine
  • N-<wbr/>Oxalylglycine
Cat No: 13944
Cayman
€33.00
Price is excluding VAT and does not include packaging neither shipping

A cell permeable inhibitor of α-ketoglutarate-dependent enzymes, including JMJD2A, JMJD2C, and JMJD2E (IC50s = 250, 500, and 24 μM, respectively); inhibits the prolyl hydroxylase domain-containing proteins PHD1 and PHD2 with IC50 values of 2.1 and 5.6 ...

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Territorial Availability: Available through Bertin Technologies only in Europe
Synonyms:
  • N-(carboxycarbonyl)-glycine
  • NOG
Correlated keywords:
  • N-oxaloglycine
  • jumonji
  • domain-containing
  • protein
  • JMJD2
  • histones
  • demethylase
  • cancers
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Product Overview:
A cell permeable inhibitor of α-ketoglutarate-dependent enzymes, including JMJD2A, JMJD2C, and JMJD2E (IC50s = 250, 500, and 24 μM, respectively); inhibits the prolyl hydroxylase domain-containing proteins PHD1 and PHD2 with IC50 values of 2.1 and 5.6 μM, respectively
The jumonji domain-containing protein 2 (JMJD2) subfamily of histone demethylases have been shown to catalyze demethylation of the methylated forms of histone 3 lysine 9 (H3K9) and H3K36 in vitro and in cells. Because histone demethylases are implicated in certain diseases, including cancer, selective inhibitors are candidate anticancer agents as well as potential tools for elucidating the biological functions of JMJDs. N-Oxalylglycine, the amide analog of α-ketoglutarate, is a cell permeable inhibitor of α-ketoglutarate-dependent enzymes, including JMJD2A, JMJD2C, and JMJD2E (IC50s = 250, 500, and 24 μM, respectively). It can also inhibit the prolyl hydroxylase domain-containing proteins PHD1 and PHD2 with IC50 values of 2.1 and 5.6 μM, respectively.
Size 5 mg
Shipping wet ice
Stability Store at -20 degrees; shelf life 730 days maximum after production
CAS Number 5262-39-5
Molecular Formula C4H5NO5
SMILES OC(C(NCC(O)=O)=O)=O
Molecular Weight 147.1
Formulation A crystalline solid
Purity ≥98%
Custom Code 2922199619
UNSPSC code 12352100

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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