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Histone H3 (21-44)-GK-biotin amide (trifluoroacetate salt)

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    Histone H3 (21-44)-GK-biotin amide (trifluoroacetate salt)
  • Histone H3 (21-44)-GK-biotin amide (trifluoroacetate salt)
Cat No: 27762
Cayman

Histone H3 (21-44)-GK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-45 of the human histone H3.3 sequence and is biotinylated via a C-terminal GK linker. Unlike histone H3.1 and H3.2, the histone H3.3 variant co...

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: 250 µg

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

Territorial Availability: Available through Bertin Technologies only in France
Synonyms:
  • L-alanyl-L-threonyl-L-lysyl-L-alanyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-alanyl-L-prolyl-L-seryl-L-threonylglycylglycyl-L-valy-L-lysyl-L-lysyl-L-prolyl-L-histidyl-L-arginyl-L-tyrosyl-L-arginyl-L-proylglycylglycyl-L-lysine-biotin amide, trifluoroacetate salt
Correlated keywords:
  • H-Ala-Thr-Lys-Ala-Ala-Arg-Lys-Ser-Ala-Pro-Ser-Thr-Gly-Gly-Val-Lys-Lys-Pro-His-Arg-Tyr-Arg-Pro-Gly-Gly-Lys(Biotin)-NH2
Product Overview:
Histone H3 (21-44)-GK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-45 of the human histone H3.3 sequence and is biotinylated via a C-terminal GK linker. Unlike histone H3.1 and H3.2, the histone H3.3 variant contains a serine residue at position 31 that is phosphorylated during late prometaphase and metaphase of mitosis.{43872} Histone H3 (21-44) also contains lysine residues at positions 23, 27, and 36 that are subject to methylation and acetylation, all of which have a role in the regulation of gene expression, and a serine residue at position 28 that is subject to phosphorylation during mitosis.{17798,45194,43872}
Size 250 µg
Shipping dry ice
Molecular Formula C127H215N45O33S • XCF3COOH
SMILES O=C(O)C(F)(F)F.O=C(NCCCC[C@@H](C(N)=O)NC(CNC(CNC([C@@H]1CCCN1C([C@H](CCCNC(N)=N)NC([C@@H](NC([C@H](CCCNC(N)=N)NC([C@@H](NC([C@@H]2CCCN2C([C@H](CCCCN)NC([C@H](CCCCN)NC([C@H](C(C)C)NC(CNC(CNC([C@@]([C@@H](C)O)([H])NC([C@H](CO)NC([C@@H]3CCCN3C([C@@H](NC([C@H
Molecular Weight 2932,4
Formulation A solid
Purity ≥95%
Custom Code 3504.00
UNSPSC code 12352100

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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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