|Other Histone Methylation Antibodies|
Histone methylation occurs with the addition of a methyl group to the amino-terminal tails of histone proteins. Depending on how many methyl groups are added and which amino acid residue is modified, histone methylation can have a positive or negative effect on gene transcription. Histone methyltransferases (HMTs) are enzymes that catalyze the addition of methyl groups to histone proteins, while histone demethylases (HDMs) remove these methyl groups. This process is important for regulating gene expression which allows different cells to express different genes.
|Histone Acetylation Antibodies|
Histone acetylation is defined by the addition of an acetyl functional group to the lysine residues of the N-terminal tail and its status can be studied with the use of histone acetylation antibodies. Evidence shows histone acetylation is highly involved in gene regulation and histone acetyltransferase (HAT) and histone deacetylase (HDAC) activity affect the availability of chromatin to gene transcription.
|Histone Deacetylation Antibodies|
Histone deacetylation, the process by which histone deacetylase (HDAC) catalyzes the removal of the acetyl functional group from histones, can be investigated using HDAC antibodies. Decreased levels of acetylation as a result of HDAC activity has been linked to repression of gene expression due to the condensed state of chromatin, referred to as heterochromatin.
|Other Histone Acetylation Antibodies|
The process of histone acetylation at lysine residues by histone acetyltransferase (HAT) is an important epigenetic marker and can be measured with the use of histone lysine acetylation antibodies. Acetylation of histones reduces the interaction of histone N termini with the phosphate groups of DNA, thereby loosening chromatin and opening it up for increased gene transcription. Acetylation of H3K14, for instance, has been linked to transcriptional activation and specifically DNA repair.
|Histone Phosphorylation Antibodies|
Antibodies that detect phosphorylated target proteins help researchers to understand the role phosphorylation plays in cellular processes. Phosphorylation can turn on and off numerous protein enzymes by adding a phosphate group to the protein, thereby affecting their activity and function.
|Ubiquitination & SUMOylation Antibodies|
Ubiquitination is the process by which ubiquitin is attached to a substrate protein after it has been made. It has been known to affect proteins by altering cellular location, impacting protein activity, and adjusting protein-protein interactions. Research shows that sumoylation regulates protein-protein interactions and subcellular targeting and is involved in numerous processes such as nuclear-cytosolic transport, apoptosis, transcriptional regulation, response to stress, protein stability, and progression through the cell cycle. Ubiquitination antibodies and sumoylation antibodies are a useful tool to researchers investigating the control mechanisms associated with numerous nuclear proteins.
|Other Histone Antibodies|
Other histone antibodies can be used to study the core nucleosomal histones, the histones regularly associated with DNA in chromatin, as well as non-canonical histone variants that often can substitute for the core histones under diverse physiological and environmental conditions. The core nucleosomal histones are mostly incorporated into chromatin during DNA replication, while histone variants can be integrated throughout the cell cycle. Adjoining of these histone variants can alter chromatin structure and affect transcription, DNA replication and other biological processes, and can influence embryonic development and cell fate decisions. Some well-known histone variants include H2A.X, H2A.Z and H3.3.
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