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Browse products name by alphabetical order:
|Cat. #||Product Name||Price|
|H10025||Histone H4 (1 - 7), N - Terminal||Inquiry|
|H10012||Histone H4 (1 - 21), p300/CBP Substrate||Inquiry|
|H10010||Histone H4 (1 - 20), PRMT7 Substrate, M1||Inquiry|
|H10004||Histone H3 (23 - 34) - Cys||Inquiry|
|H10002||Histone H3 (23 - 34)||Inquiry|
|H10018||Histone H3 (21 - 44)||Inquiry|
|H10020||Histone H3 (15.39)||Inquiry|
|H10019||Histone H3 (116.136), C116.136||Inquiry|
|H10023||Histone H3 (1 - 25), amide||Inquiry|
|H10016||Histone H3 (1 - 21), N - Terminal||Inquiry|
|H10014||Histone H3 (1 - 20), N - Terminal||Inquiry|
|H10011||Histone H2A (1 - 20)||Inquiry|
|H10017||Histone H1. (22 - 42), human, mouse||Inquiry|
|H10005||Histone H1 - derived Peptide||Inquiry|
|H10001||Histone 4 - 12, p300/CBP Substrate||Inquiry|
In eukaryotic cells, the basic unit of chromatin is the nucleosome, which is composed of histones (H2A, H2B, H3 and H4), H1, and DNA. Histone peptides not only regulate gene expression, but also play an important role in DNA damage repair, replication and recombination. With the development of epigenetics, the role of histone peptides becomes more and more important. Histone peptides function mainly through a variety of epigenetic modifications. Histone modification includes acetylation and deacetylation, methylation and demethylation, phosphorylation and dephosphorylation, ubiquitination and deubiquitination, and etc.
Mechanism of action
Acetylation and methylation are two important modifications of histone peptides, the acetylation is regulated commonly by histone acetyltransferases and histone deacetylases, these two enzymes modify histone peptides reversibility to regulate histone acetylation level, thus to regulate the initiation and extension of transcription. The acetylation promotes transcription, on the contrary, the deacetylation inhibits transcription. Moreover, the histone methylation mainly occurs on lysine and arginine residues of H3 and H4, which is regulated by histone methyltransferase and histone demethylase.
Application of Histone Peptides
The acetylated histone peptides inhibit the formation of many tumor cells, including the adenocarcinoma cell of rectum, the gastric cancer cell, the breast cancer cell, and the prostate cancer cells. And balancing the acetylation of histone peptides contributes to the treatment of diabetes. This is because the deacetylation of histone peptides plays a negative role in islet development, beta cell proliferation and beta cell functional regulation. Methylated histone peptides and demethylated histone peptides are also involved in a variety of diseases. One histone demethylase named JHDM1B is considered as a tumor suppressor. In addition, there are several kinds of different histone methyltransferases has been linked to heart disease, such as SymD1, EMHT1 and Dot1. The abnormality of SymD1 led to a developmental disorder of embryonic cardiomyocytes. The mutation or deletion of EMHT1 is the main cause of 9qSTDS syndrome. When cells differentiate, the absence of Dot1 results in a variety of developmental abnormalities, including heart malformation. In a word, the histone peptides are associated with a variety of human diseases, and whether it plays a positive role or a negative role depends on different superficial modification.
1. Jennifer S. Carew., Francis J. Giles., Steffan T. Nawrocki. (2008). Histone deacetylase inhibitors: Mechanisms of cell death and promise in combination cancer therapy. Cancer letters, 269(1), 7-17.
2. L Morera., M Lübbert., M Jung. (2016). Targeting histone methyltransferases and demethylases in clinical trials for cancer therapy. Clinical Epigenetics, 8(1), 5-7.