histone h3 (121)

Histone H3 (1-21) is a truncated form of the Histone H3 protein consisting of amino acids 1 to 21. It serves as a common substrate for methyltransferase assays targeting Histone 3 at lysine 4 and lysine 9, as well as for acetyltransferase assays targeting Histone 3 at lysine 9 and lysine 14.

Histone H3 (1-35) acetate is a 35-residue peptide of histone H3. Histone H3 is an important protein that plays a role in the dynamic and long term regulation of genes.

Histone H3 (1-25), amide is a N-terminal peptide fragment of histone H3 that serves as a substrate for histone methyltransferases (HMTs). It is utilized to identify the substrate for HMTs and proves to be more efficient than histone H3 (15-39) and full-length histone H3 for the HMT G9a.

H-Phe(3-CN)-OH (catalog number: T66059, CAS number: 57213-48-6) is a valuable organic compound for life sciences research.

Histone H3 (5-23), a derivative of histone H3 consisting of amino acids 5-23, serves as a substrate for histone acetyltransferase (HAT) assays.

H-D-Phe(3-Br)-OH is a useful organic compound for research related to life sciences. The catalog number is T66311 and the CAS number is 99295-78-0.

Histone H3 (116-136), also known as C116-136, is a peptide comprising amino acids 116 to 136 of the C-terminus of histone H3.

H-D-Phe(3-F)-OH, with catalog number T67306 and CAS number 110117-84-5, is a valuable organic compound for research in life sciences.

H-DL-Phe(3-Br)-OH is a useful organic compound for research related to life sciences. The catalog number is T66042 and the CAS number is 30163-20-3.

Histone H3 (1-35) is a 35-residue peptide derived from histone H3, a crucial component of the five main histones involved in chromatin formation within eukaryotic cells.

Histone H3 (21-44), derived from the 21-44 amino acid sequence of histone H3, is commonly used as a substrate in protein arginine methyltransferase assays to analyze methylation activity.

Histone H3 (23-34) is a peptide composed of amino acid residues 23 to 34 of the histone H3 protein, including lysine residues at positions 23 and 27, which are subject to methylation and acetylation modifications.