Recombinant Human YTHDF3 protein
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(1 Publication)
Recombinant Human YTHDF3 protein is a Human Full Length protein, in the 1 to 585 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
YTH domain-containing family protein 3, DF3, YTHDF3
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human YTHDF3 protein (AB166020)
ab166020 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
YTHDF3 facilitates the process of mRNA metabolism by participating in the regulation of mRNA translation and degradation. It functions as part of a dynamic complex with YTHDF1 and YTHDF2 coordinating the fate of m6A-modified mRNAs. YTHDF3 supports mRNA decay in synergy with YTHDF2 and enhances translation efficiency in cooperation with YTHDF1. This involvement in regulating gene expression at the post-transcriptional level equips cells to respond rapidly to various stimuli aligning gene expression with cellular needs.
Pathways
YTHDF3 significantly impacts RNA processing and metabolism pathways. YTHDF3 together with YTHDF1 and YTHDF2 modulates the m6A-mediated mRNA decay pathway. It holds functional significance in the cellular response to stress and adaptations in energy metabolism. YTHDF3 interacts closely with proteins such as IGF2BP1 alongside the YTHDF proteins which are critical in maintaining RNA stability and translation thereby illustrating its role across significant cellular pathways.
Specifications
Form
Liquid
General info
Function
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed : 28106072, PubMed : 28106076, PubMed : 28281539, PubMed : 32492408). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed : 22575960, PubMed : 24284625, PubMed : 28106072, PubMed : 28281539, PubMed : 32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3 (PubMed : 32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed : 28106072, PubMed : 28106076, PubMed : 32492408). Acts as a negative regulator of type I interferon response by down-regulating interferon-stimulated genes (ISGs) expression : acts by binding to FOXO3 mRNAs (By similarity). Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification (By similarity). Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation (PubMed : 28106072). Recognizes and binds m6A-containing circular RNAs (circRNAs); circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons (PubMed : 28281539). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues : polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed : 31292544, PubMed : 31388144, PubMed : 32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed : 31292544). May also recognize and bind N1-methyladenosine (m1A)-containing mRNAs : inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation (PubMed : 32194978).. Has some antiviral activity against HIV-1 virus : incorporated into HIV-1 particles in a nucleocapsid-dependent manner and reduces viral infectivity in the next cycle of infection (PubMed : 32053707). May interfere with this early step of the viral life cycle by binding to N6-methyladenosine (m6A) modified sites on the HIV-1 RNA genome (PubMed : 32053707).
Sequence similarities
Belongs to the YTHDF family. YTHDF3 subfamily.
Post-translational modifications
(Microbial infection) Proteolytically cleaved by HIV-1 protease when incorporated into HIV-1 particles in a nucleocapsid-dependent-manner. Cleavage by HIV-1 protease probably ensures optimal infectivity of the mature virion.
Target data
Publications (1)
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Molecular cancer 22:202 PubMed38087322
2023
Applications
Unspecified application
Species
Unspecified reactive species
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