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Cat No | BSPA-0529 |
Conjugate | |
Type | Polyclonal Antibody |
Source | Rabbit |
Size | 1 mg |
Application | WB; IHC-F; IHC-P; ICC/IF; ELISA |
Format | Liquid |
Concentration | Please refer to the vial lable for the specific concentration. |
Buffer | Supplied in PBS. |
Storage | Store at -20 degree. Avoid repeted freeze/thaw cycl. |
Synonyms | H3 histone antibody, HIST1H3A antibody, Histone cluster 1, H3a antibody |
Purification | |
Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
MolecularWeight | |
Description | |
Background | The nucleosome, made up of four core histone proteins , is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination. Histone acetylation occurs mainly on the amino-terminal tail domains of histones H2A , H2B , H3 , and H4 and is important for the regulation of histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair. Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the accessibility of DNA to various DNA-binding proteins. In addition, acetylation of specific lysine residues creates docking sites for a protein module called the bromodomain, which binds to acetylated lysine residues. Many transcription and chromatin regulatory proteins contain bromodomains and may be recruited to gene promoters, in part, through binding of acetylated histone tails. Histone acetylation is mediated by histone acetyltransferases , such as CBP/p300, GCN5L2, PCAF, and Tip60, which are recruited to genes by DNA-bound protein factors to facilitate transcriptional activation. Deacetylation, which is mediated by histone deacetylases , reverses the effects of acetylation and generally facilitates transcriptional repression. |