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Citrullinated Glucose-6-phosphate Isomerase (human, recombinant)

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    Citrullinated Glucose-6-phosphate Isomerase (human, recombinant)
  • Citrullinated Glucose-6-phosphate Isomerase (human, recombinant)
Cat No: 30967
Proteins - Enzymes
Cayman

Glucose-6-phosphate isomerase (GPI) is a glycolytic enzyme that catalyzes the conversion of D-glucose-6-phosphate (Item No. 20376) to D-fructose-6-phosphate (Item No. 19588).{60225,60226} It exists as a dimer where each monomer is composed of a large ...

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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:
  • Phosphohexose Sperm Antigen 36 SA-36 Padi PAD-4 auto-antigen Autocrine Motility Factor Neuroleukin AMF NLK G6P
Product Overview:
Glucose-6-phosphate isomerase (GPI) is a glycolytic enzyme that catalyzes the conversion of D-glucose-6-phosphate (Item No. 20376) to D-fructose-6-phosphate (Item No. 19588).{60225,60226} It exists as a dimer where each monomer is composed of a large and small globular domain, which form a cleft that contains the catalytic active site, and a C-terminal tail.{60226,60227} GPI is ubiquitously expressed and localized to the cytoplasm.{60225,60226} It also functions as a neurotrophic growth factor and has a role in immunoglobulin synthesis.{60226} GPI is an autoantigen in rheumatoid arthritis (RA).{59168} Immunization with recombinant human GPI induces inflammatory cell infiltration, cartilage destruction, and bone erosion in the inflamed joints of mice, an effect that is reduced in Padi4 knockout mice, which lack peptidyl arginine deiminase 4 (PAD4), an enzyme involved in protein citrullination.{60228} Citrullinated GPI autoantibodies have been found in the serum of patients RA.{59168}
Size 100 µg
Shipping dry ice
Formulation 25 mM Tris, pH 7.0, with 100 mM sodium chloride, and 10% glycerol
Purity ≥90% estimated by SDS-PAGE
Custom Code 3504.00
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.

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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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