This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the comfort when using this website, are used for direct advertising or to facilitate interaction with other websites and social networks, are only set with your consent.
Configuration
Technically required
These cookies are necessary for the basic functions of the shop.
"Allow all cookies" cookie
"Decline all cookies" cookie
CSRF token
Cookie preferences
Currency change
Customer-specific caching
FACT-Finder tracking
Individual prices
Selected shop
Session
Comfort functions
These cookies are used to make the shopping experience even more appealing, for example for the recognition of the visitor.
Note
Show the facebook fanpage in the right blod sidebar
Statistics & Tracking
Affiliate program
Conversion and usertracking via Google Tag Manager
The human ASH2L gene encodes a 628 amino acid protein known as ASH2L1, or isoform 1, which contains a nuclear localization signal and PHD finger motif, suggesting that the gene product functions as a transcription regulator. Alternative splicing results in a shorter isoform 2, designated ASH2L2, which is missing the first 94 amino acid residues found in ASH2L1. Human ASH2L proteins are 60% homologous to Drosophila ash2, which positively regulates expression of certain genes in early development, and contain similar, but not identical, domains, including a zinc finger motif. ASH2L is highly expressed in fetal liver, testis and leukemia cell lines with erythroid and megakaryocytic potential, such as K562, Hel and Dami. Protein function: Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis. [The UniProt Consortium]
This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the usability of this website, serve for direct advertising or simplify interaction with other websites and social networks, will only be used with your consent.
More information