Recombinant Human YTHDC1 protein (GST tag N-Terminus)
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Recombinant Human YTHDC1 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 709 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
KIAA1966, YT521, YTHDC1, YTH domain-containing protein 1, Splicing factor YT521, YT521-B
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human YTHDC1 protein (GST tag N-Terminus) (AB164876)
ab164876 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
YTHDC1 operates in the regulation of mRNA splicing and transportation. It associates with spliceosome components to influence alternative splicing decisions. YTHDC1 part of the m6A reader complex recognizes the m6A methylation mark on RNA aiding in the control of mRNA fate. Additionally its interactions with certain proteins affect RNA stability and translation essential for proper gene expression regulation.
Pathways
YTHDC1 plays a significant role in RNA metabolism and the cellular response to stress. Involvement in the mRNA splicing pathway highlights its contribution to gene expression regulation. YTHDC1 interacts with proteins like SRSF3 and SRFS10 which modulate RNA splicing and stability. Another pathway includes its role in the cellular stress response where YTHDC1 helps maintain RNA integrity linking it to adaptive responses in cells.
Specifications
Form
Liquid
General info
Function
Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed : 25242552, PubMed : 26318451, PubMed : 26876937, PubMed : 28984244). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed : 25242552, PubMed : 26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed : 26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed : 26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping : this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed : 26876937). May also regulate alternative splice site selection (PubMed : 20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3 : interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed : 28984244). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed : 27602518). Involved in random X inactivation mediated by Xist RNA : recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed : 27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed : 32663306). Involved in germline development : required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). Independently of its N6-methyladenosine-containing RNA reader activity, it regulates PPARG stability by preventing its interaction with the E3 ubiquitin ligase ARIH2, thereby protecting it from ubiquitin-mediated proteasomal degradation and contributing to brown adipose tissue (BAT) development and energy homeostasis (By similarity).
Post-translational modifications
Tyrosine phosphorylated.
Subcellular localisation
Nucleus
Target data
Product promise
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