Rabbit Anti-SETD2 Polyclonal Antibody#abs136758

abs136758-100ug

1-2 Weeks

301.0

abs136758-50ug

1-2 Weeks

201.0

catalog

Description

Huntington's disease (HD) is a neurodegenerative disorder characterized by the progressive loss of striatal neurons. The underlying cause of this devastating condition is an expansion of the polyglutamine tract in the huntingtin protein, encoded by the HD gene. This gene is responsible for producing a protein that belongs to a group of huntingtin interacting proteins known for their WW motifs.
Interestingly, the huntingtin protein is not just any ordinary protein. It serves as a histone methyltransferase, specifically targeting lysine-36 of histone H3. Methylation of this particular residue is closely linked to active chromatin, which plays a crucial role in gene expression.
But that's not all - this protein also has an intriguing feature. It possesses a unique transcriptional activation domain, contributing to its involvement in gene regulation. Furthermore, it has been discovered in association with hyperphosphorylated RNA polymerase II, a key component in the transcription process.
In summary, Huntington's disease arises from an expansion of the polyglutamine tract in the huntingtin protein. This protein, characterized by its WW motifs, functions as a histone methyltransferase targeting lysine-36 of histone H3. Its ability to methylate this residue is linked to active chromatin, influencing gene expression. Additionally, it possesses a transcriptional activation domain and has been observed alongside hyperphosphorylated RNA polymerase II. This complex interplay of cellular mechanisms underlies the pathology of Huntington's disease.

Concentration

1mg/ml

Target

Background

Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation. Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A. Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction. H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A. H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase. Required during angiogenesis. Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression. Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3) (PubMed:27518565). Alpha-TubK40me3 is required for normal mitosis and cytokinesis and is proposed to be a specific tag in cytoskeletal remodeling (PubMed:27518565).