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15-Lipoxygenase-2 (human, recombinant)

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    15-<wbr/>Lipoxygenase-<wbr/>2 (human, recombinant)
  • 15-<wbr/>Lipoxygenase-<wbr/>2 (human, recombinant)
Cat No: 10011263
Proteins - Enzymes
Cayman

Two types of 15-lipoxygenase (15-LO) have been discovered and characterized, both of which metabolize arachidonic acid (AA) to produce 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE). 15-LO-1 oxygenates AA at both C-15 and C-12, whereas 15-LO-2 exclus...

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: 100 µg

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

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • arachidonic acids recombinant proteins 15-HETE 15-HpETE active ferroptosis
Product Overview:
Two types of 15-lipoxygenase (15-LO) have been discovered and characterized, both of which metabolize arachidonic acid (AA) to produce 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE). 15-LO-1 oxygenates AA at both C-15 and C-12, whereas 15-LO-2 exclusively oxygenates C-15 of AA.{11792,4675} Human 15-LO-2 has a molecular mass of approximately 76 kDa and exhibits approximately 40% identity to the reticulocyte 15-LO-1.{4675,11789} Expression of 15-LO-2 appears to be restricted to prostate, lung, skin, and cornea and may play a role in the normal development of these tissues.{11790} The protein levels and enzymatic activity of 15-LO-2 are both down-regulated in prostate cancer compared with normal and benign prostate tissues, implicating a possible protective role for 15-LO-2 against tumor formation.{11790,8774,9075} Cayman's 15-LO-2 (human, recombinant) is expressed and purified from E. coli. The purity was determined using gel electrophoresis followed by coomassie staining. 15-LO-2 specific activity was established using arachidonic acid as the substrate and monitoring diene formation by measuring absorbance 236 nm.
Size 100 µg
Shipping dry ice
Formulation PBS, pH 7.5, with 1 mM DTT, 20% glycerol
Purity ≥85% 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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