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Gcn5 (human recombinant)

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    Gcn5 (human recombinant)
  • Gcn5 (human recombinant)
Cat No: 10782
Proteins - Enzymes
Cayman
€469.00
Price is excluding VAT and does not include packaging neither shipping

Gcn5 and PCAF are highly homologous members of the Gcn5-related N-acetyltransferase (GNAT) superfamily of N-acetyltransferases involved in histone acetylation.{20191} Gcn5 and PCAF contain a highly conserved central core with divergent N- and C-termin...

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: 100 µg

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

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Territorial Availability: Available through Bertin Pharma only in Europe
Correlated keywords:
  • epigenetics modifications histones acetylation cancers GNAT N-acetyltransferases enzymes STAGA TFTC SAGA ATAC H3K14 H3K9 H3K18 H4K8 H4K16 H3 H2B KAT2B p300/CBP associated factors Spt-Ada-GCN5-aceytltransferase Ada Two-A containing CoASH Gcn-5 N-acetyltransferases enzymatic subunits complexes proteins active
Product Overview:
Gcn5 and PCAF are highly homologous members of the Gcn5-related N-acetyltransferase (GNAT) superfamily of N-acetyltransferases involved in histone acetylation.{20191} Gcn5 and PCAF contain a highly conserved central core with divergent N- and C-terminal ends.{20189} Gcn5/PCAF are enzymatic subunits that exist in a mutually exclusive manner as part of the mammalian SAGA and ATAC complexes.{20187,20188} Recombinant Gcn5 preferentially acetylates lysine 14 on histone H3 in vitro. Recombinant Gcn5 alone is unable to acetylate nucleosomal core histone substrates. Acetylation of the nucleosomal histones requires that Gcn5 be a part of either the multisubunit SAGA or ATAC protein complexes.{20190} The multisubunit Gcn5/PCAF-containing complexes have a broad substrate specificity, including H3K9, H3K18, H4K8, and H4K16, as well as additional sites on histone H2B.{20187}
Size 100 µg
Shipping dry ice
Stability Store at -80 degrees; shelf life 730 days
Formulation 50 mM Tris-HCl, pH 8.0, containing 150 mM sodium chloride and 20% glycerol
Purity ≥50 % (estimated by SDS-PAGE)
Custom Code 3504.00
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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