gene exp ythdc2 hs00403320 m1 (Thermo Fisher)
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gene exp ythdc2 hs00403320 m1
![Clinical characteristics of patients with <t> YTHDC2 </t> variants]()
Gene Exp Ythdc2 Hs00403320 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ythdc2/Gene+Exp%2E+YTHDC2%2C+Hs00403320_m1/pmc08983136-182-43-47
Average 91 stars, based on 1 article reviews
Gene Exp Ythdc2 Hs00403320 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ythdc2/Gene+Exp%2E+YTHDC2%2C+Hs00403320_m1/pmc08983136-182-43-47
Average 91 stars, based on 1 article reviews
gene exp ythdc2 hs00403320 m1 - by Bioz Stars,
2026-08
91/100 stars
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1) Product Images from "Pathogenic variants in the human m 6 A reader YTHDC2 are associated with primary ovarian insufficiency"
Article Title: Pathogenic variants in the human m 6 A reader YTHDC2 are associated with primary ovarian insufficiency
Journal: JCI Insight
doi: 10.1172/jci.insight.154671
Figure Legend Snippet: Clinical characteristics of patients with YTHDC2 variants
Techniques Used:
Figure Legend Snippet: ( A ) Pedigrees of kindred with YTHDC2 variants (upper panel: p.P856R, lower panel: p.E377*). Solid symbols indicate affected family members. Genotype is indicated underneath tested family members. ( B ) Domains of the human YTHDC2 protein. Domains include an R3H domain; 2 RecA-like domains, RecA1: ATP-binding DEAD-like helicase domain (DExDc) and RecA2: helicase superfamily C-terminal domain (HELICc); 2 ankyrin repeats (506–535 and 539–568) comprising the ankyrin domain (ANK); a helicase-associated domain (HA2), an oligonucleotide/oligosaccharide-binding fold domain (OB-fold), and a YTH (YT521-B homology) m 6 A-dependent RNA binding domain (YTH). The DExDc, ankyrin repeats, and HELICc domains make up the helicase core of this protein. Domain positions (in amino acids) are annotated below the schematic. The position of the 2 pathogenic variants (p.E377*; p.P856R); the ketu mouse mutation (mouse: p.H327R; human: p.H312R) (Jain et al. 2017, ref. ); and another Ythdc2 –/– knockout mouse (deletion of 50 amino acids within exon 7) (Wojtas et al. 2017, ref. ) are indicated. ( C ) Amino acid conservancy in the region of YTHDC2 surrounding codon 856. Yellow asterisks represent complete conservation among the species shown. ( D ) The m 6 A methyltransferase complex. The m 6 A modification on mRNA is mediated by “writers” and demethylases (“erasers”). “Readers” recognize the m 6 A modification and allow execution of its functions. One key reader is YTHDC2 , with its known cofactors MEIOC and XRN .
Techniques Used: Binding Assay, RNA Binding Assay, Mutagenesis, Knock-Out, Modification
Figure Legend Snippet: ( A ) Violin plots depicting normalized counts for YTHDC2 , MEIOC , and XRN1 in the developing ovary and testis at 4 developmental stages (4 samples at stages CS22/23, 9 wpc, 11 wpc, 15/16 wpc). ( B ) Quantitative reverse transcriptase PCR (qRT-PCR) expression (log 2 ) of YTHDC2 in developing ovary and testis compared with reference ( ACTB ) and relative to expression in an index CS22 ovary sample. Four fetal ovary and fetal testis samples were included at CS22/CS23, 9 wpc, 11 wpc, 15/16 wpc, and 19/20 wpc. ( C ) qRT-PCR expression (log 2 ) of MEIOC in developing ovary and testis compared with reference ( ACTB ) and relative to the expression in a CS22 ovary sample. Four fetal ovary and fetal testis samples were included at CS22/CS23, 9 wpc, 11 wpc, 15/16 wpc, and 19/20 wpc. ( D ) qRT-PCR mean expression (log 2 ) of YTHDC2 in 4 adult ovary samples and 4 adult testis samples from individuals without gonadal insufficiency. B – D represent mean expression of triplicates, and error bars indicate mean ± SEM. qRT-PCR experiments were performed 3 times; representative data from 1 experiment shown. Differences in mean expression between sample groups were assessed using multiple t test analysis (* P < 0.05; ** P < 0.01); correction for multiple comparisons was performed using Holm-Šídák. CS, Carnegie stage. ( E ) Uniform manifold approximation and projection representation of distinct germ cell clusters ( n = 8867 germ cells) identified by single-cell RNA sequencing of human fetal gonads between 6 and 21 wpc. Key ovary clusters are annotated. PGCs, primordial germ cells; GCs, germ cells. ( F ) Visium spatial transcriptomic expression of YTHDC2 in a 17 wpc human fetal ovary. EG, extragonadal. ( G ) Immunohistochemistry of YTHDC2 in a 16 wpc human fetal ovary showing increased staining in the central region containing meiotic cells and decreased staining in primordial germ cells at the periphery in the cortex of the fetal ovary (PGCs).
Techniques Used: Reverse Transcription, Quantitative RT-PCR, Expressing, RNA Sequencing, Immunohistochemistry, Staining
Figure Legend Snippet: ( A ) qRT-PCR mean expression (log 2 ) of YTHDC2 , SYCP2L , and TRIM9 in the peripheral leukocytes of patients with p.P856R (missense) and p.E377* (nonsense) YTHDC2 variants compared with reference ( ACTB ) and relative to the expression in patients with POI who have no known YTHDC2 variants. Samples were processed in triplicate and error bars indicate mean ± SEM (** P < 0.01, ANOVA 1 way comparing gene expression between the 3 groups). Experiments were performed 3 times and representative data from 1 experiment are shown. ( B ) Cellular localization studies of either WT or mutant p.P856R YTHDC2 together with MEIOC in HeLa cells. Original magnification, ×100.
Techniques Used: Quantitative RT-PCR, Expressing, Gene Expression, Mutagenesis
Figure Legend Snippet: ( A ) The HA2 domain is shown in green and codon P856 is indicated by an arrow. The RNA-binding domain is shown with the bound RNA in orange. ( B ) P856R can establish strong hydrogen bond interactions with surrounding residues (D855,T859, Q905, Q908, R937, R959, N967), which is predicted to increase stability and to reduce flexibility of the P856R protein. ( C ) The radius of gyration (RoG) indicates that P856R mutant protein is more compact than WT protein (left panel), and there is an increased number of protein-RNA hydrogen bonds in the P856R protein compared with WT (right panel), suggesting the P856R protein to be more stable and less flexible than WT. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. **** P < 0.0001, unpaired t test. ( D ) Root-mean square deviation (RMSD) of alpha carbons at the protein and nucleic acid (NA) level for both WT and P856R mutant YTHDC2. Global movement is lower in the P856R mutant protein compared with WT. ( E ) Replacement of proline at position 856 with arginine may also alter the electrostatic charge of YTHDC2.
Techniques Used: RNA Binding Assay, Mutagenesis
Figure Legend Snippet: Although the exact role of partners is still incompletely understood, the YTHDC2-MEIOC-XRN1 complex would stabilize meiotic transcripts and/or degrade mitotic transcripts by binding to m 6 A-marked mRNA, promoting a normal mitosis to meiosis transition. At pachytene, YTHDC2 and other DExH helicases may functionally partner with PIWIL proteins within cytoplasmic RNA germ cell granules and may regulate piRNA activity, which is required for normal meiotic timing and progression.
Techniques Used: Binding Assay, Activity Assay
