YTHDF3 Antibody
(Synonyms: YTH domain-containing family protein 3, DF3, YTHDF3)YTHDF3 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to YTHDF3.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:50-200 |
Product Details
YTHDF3 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to YTHDF3.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 64 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 63 kDa
Purified recombinant protein of human YTHDF3.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
YTHDF3 is a Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3. The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. 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. 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. 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. The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules. May also recognize and bind N1-methyladenosine (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation[1][2][3][4][5][6][7][8][9][10].
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Subcellular Localization
Cytoplasm, cytosol; Cytoplasm, P-body; Cytoplasm, Stress granule
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Expression
Induction: Following heat shock stress. -
Isoforms & Post-Translational Modification
YTHDF3 has an amino acid length of 585, molecular weight is 63861 Da.
(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. -
Subunit
Interacts with CNOT1; promoting recruitment of the CCR4-NOT complex.
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SwissProt ID
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Synonyms
YTH domain-containing family protein 3, DF3, YTHDF3
Documentation
[1]. Shi H, et al. YTHDF3 facilitates translation and decay of N(6)-methyladenosine-modified RNA. Cell Res. 2017 Mar;27(3):315-328. [Content Brief]
[2]. Li A, et al. Cytoplasmic m(6)A reader YTHDF3 promotes mRNA translation. Cell Res. 2017 Mar;27(3):444-447. [Content Brief]
[3]. Yang Y, et al. Extensive translation of circular RNAs driven by N(6)-methyladenosine. Cell Res. 2017 May;27(5):626-641. [Content Brief]
[4]. Zaccara S, et al. A Unified Model for the Function of YTHDF Proteins in Regulating m(6)A-Modified mRNA. Cell. 2020 Jun 25;181(7):1582-1595.e18. [Content Brief]
[5]. Dominissini D, et al. Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq. Nature. 2012 Apr 29;485(7397):201-6. [Content Brief]
[6]. Wang X, et al. N6-methyladenosine-dependent regulation of messenger RNA stability. Nature. 2014 Jan 2;505(7481):117-20. [Content Brief]
[7]. Ries RJ, et al. m(6)A enhances the phase separation potential of mRNA. Nature. 2019 Jul;571(7765):424-428. [Content Brief]
[8]. Gao Y, et al. Multivalent m(6)A motifs promote phase separation of YTHDF proteins. Cell Res. 2019 Sep;29(9):767-769. [Content Brief]
[9]. Fu Y, et al. m(6)A-binding YTHDF proteins promote stress granule formation. Nat Chem Biol. 2020 Sep;16(9):955-963. [Content Brief]
[10]. Zheng Q, et al. Cytoplasmic m(1)A reader YTHDF3 inhibits trophoblast invasion by downregulation of m(1)A-methylated IGF1R. Cell Discov. 2020;6:12. [Content Brief]