YTHDF3 Antibody (Rabbit mAb) [P16G5]

Application: Reactivity: Human, Mouse, Rat, Monkey

Usage Information

Dilution
WB1:1000-1:5000 IP1:100 IF1:3200

Application
WB, IP, IF

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
64 kDa N/A
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Mouse colon tissue; Mouse cerebellum tissue; Mouse hippocampus tissue; T-47D cells; HCT-116 cells; Neuro-2a cells; NIH/3T3 cells; C6 cells; COS-7 cells; 293T cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
YTHDF3 Antibody (Rabbit mAb) [P16G5] detects endogenous levels of total YTHDF3 protein.

Clone
P16G5

Synonym(s)
FLJ31657; YTH domain family 3; YTH domain family protein 3; YTH domain family, member 3; YTH N6-methyladenosine RNA binding protein 3; YTHD3; YTHDF3

Background
YTHDF3 belongs to the YTH domain-containing family of N6-methyladenosine readers, sitting alongside YTHDF1 and YTHDF2 as one of three cytoplasmic paralogs that share a conserved C-terminal YTH domain for m6A recognition and an intrinsically disordered N-terminal region that mediates protein-protein interactions and subcellular localization. YTHDF3 recognizes m6A-methylated transcripts and channels them toward the translation machinery through direct interaction with components of the 40S and 60S ribosomal subunits, physically bridging methylated mRNA to actively translating ribosomes. This activity operates in close cooperation with YTHDF1: the two proteins share a substantial overlap in bound transcripts, and depletion of either protein reduces the RNA-binding capacity of the other, indicating a coordinated rather than independent mode of target selection. Transcripts bound jointly by YTHDF1 and YTHDF3 show markedly higher translation efficiency than those bound by either protein alone, and loss of YTHDF3 lowers nascent protein output from its methylated targets, establishing translation enhancement as its principal cytoplasmic role. YTHDF3 also displays autoregulatory behavior, binding m6A sites within its own 5' untranslated region to drive cap-independent translation of its own transcript, a feed-forward mechanism that amplifies its cellular abundance under permissive conditions. This translation-promoting function extends into pathological settings, where YTHDF3 overexpression enhances translation of m6A-enriched transcripts encoding ST6GALNAC5, GJA1, EGFR, and VEGFA, genes that govern tumor cell interaction with brain endothelium, blood-brain barrier crossing, and angiogenesis, and elevated YTHDF3 expression correlates with brain metastasis and gene copy number gain in breast cancer. Selective enrichment for m6A-marked ribosome-associated transcripts, together with its dual role in normal translational enhancement and disease-associated target engagement, positions YTHDF3 as a tractable node for probing m6A-dependent translational control and tumor progression across tissue contexts.

Background

YTHDF3 belongs to the YTH domain-containing family of N6-methyladenosine readers, sitting alongside YTHDF1 and YTHDF2 as one of three cytoplasmic paralogs that share a conserved C-terminal YTH domain for m6A recognition and an intrinsically disordered N-terminal region that mediates protein-protein interactions and subcellular localization. YTHDF3 recognizes m6A-methylated transcripts and channels them toward the translation machinery through direct interaction with components of the 40S and 60S ribosomal subunits, physically bridging methylated mRNA to actively translating ribosomes. This activity operates in close cooperation with YTHDF1: the two proteins share a substantial overlap in bound transcripts, and depletion of either protein reduces the RNA-binding capacity of the other, indicating a coordinated rather than independent mode of target selection. Transcripts bound jointly by YTHDF1 and YTHDF3 show markedly higher translation efficiency than those bound by either protein alone, and loss of YTHDF3 lowers nascent protein output from its methylated targets, establishing translation enhancement as its principal cytoplasmic role. YTHDF3 also displays autoregulatory behavior, binding m6A sites within its own 5' untranslated region to drive cap-independent translation of its own transcript, a feed-forward mechanism that amplifies its cellular abundance under permissive conditions. This translation-promoting function extends into pathological settings, where YTHDF3 overexpression enhances translation of m6A-enriched transcripts encoding ST6GALNAC5, GJA1, EGFR, and VEGFA, genes that govern tumor cell interaction with brain endothelium, blood-brain barrier crossing, and angiogenesis, and elevated YTHDF3 expression correlates with brain metastasis and gene copy number gain in breast cancer. Selective enrichment for m6A-marked ribosome-associated transcripts, together with its dual role in normal translational enhancement and disease-associated target engagement, positions YTHDF3 as a tractable node for probing m6A-dependent translational control and tumor progression across tissue contexts.

References
https://pubmed.ncbi.nlm.nih.gov/28106076/ https://pubmed.ncbi.nlm.nih.gov/33125861/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%