Histone H3K27Ac (21-43)-GGK-biot

Confirm delete?

Histone H3K27Ac (21-43)-GGK-biotin (trifluoroacetate salt)

Zoom

Cat No: 27763

Histone H3K27Ac (21-43)-GGK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-44 of the human histone H3.1 and H3.2 sequences. It is acetylated at lysine 27 and biotinylated via a C-terminal GGK linker. Acetylation ...

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

Product Overview
Data
Downloads
About Cayman

Territorial Availability: Available through Bertin Technologies only in France

Synonyms:

L-alanyl-L-threonyl-L-lysyl-L-alanyl-L-alanyl-L-arginyl-N6-acetyl-L-lysyl-L-seryl-L-alanyl-L-prolyl-L-alanyl-L-threonylglycylglycyl-L-valyl-L-lysyl-L-lysyl-L-prolyl-L-histidyl-L-arginyl-L-tyrosyl-L-arginyl-L-prolylglycylglycyl-L-lysine-biotin, trifluoroacetate salt

Correlated keywords:

H-3 H-Ala-Thr-Lys-Ala-Ala-Arg-Lys(Ac)-Ser-Ala-Pro-Ala-Thr-Gly-Gly-Val-Lys-Lys-Pro-His-Arg-Tyr-Arg-Pro-Gly-Gly-Lys(Biotin)-OH H3K-27Ac H3K27-Ac K-4 ATKAARKAcSAPATGGVKKPHRYRPGGK Lys(Ac)-27 TFA mono- tri-methylation

Product Overview:
Histone H3K27Ac (21-43)-GGK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-44 of the human histone H3.1 and H3.2 sequences. It is acetylated at lysine 27 and biotinylated via a C-terminal GGK linker. Acetylation of histone H3 at lysine 27 is associated with active gene transcription.{46252} H3K27 acetylation and H3K4 monomethylation are enriched near active enhancers and H3K27 acetylation and H3K4 trimethylation together mark transcription start sites of actively transcribed genes.

Size	250 µg
Shipping	dry ice
Molecular Formula	C₁₂₉H₂₁₆N₄₄O₃₄S • XCF₃COOH
SMILES	O=C(O)C(F)(F)F.CC(NCCCC[C@@H](C(N[C@@H](CO)C(N[C@H](C(N1CCC[C@H]1C(N[C@H](C(N[C@]([C@@H](C)O)([H])C(NCC(NCC(N[C@@H](C(C)C)C(N[C@@H](CCCCN)C(N[C@@H](CCCCN)C(N2CCC[C@H]2C(N[C@H](C(N[C@@H](CCCNC(N)=N)C(N[C@H](C(N[C@@H](CCCNC(N)=N)C(N3CCC[C@H]3C(NCC(NCC(N[C@@
Molecular Weight	2959,5
Formulation	A solid
Purity	≥95%
Custom Code	3504.00
UNSPSC code	12352100

Technical File

MSDS

Click here to ask for your quote and get 15% off Cayman's products.

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.