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Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. Zusätzlich bieten wir Ihnen TDRD3 Proteine (3) und und viele weitere Produktgruppen zu diesem Protein an.
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Structural basis of the interaction between TOP3B (zeige TOP3B Antikörper) and the TDRD3 auxiliary factor has been reported.
Top3b (zeige TOP3B Antikörper) proteins from several animals associate with polyribosomes, which are units of mRNA translation, whereas the Top3 (zeige TOP3A Antikörper) homologs from E. coli and yeast lack the association. The Top3b (zeige TOP3B Antikörper)-polyribosome association requires TDRD3, which directly interacts with Top3beta and is present in animals but not bacteria or yeast.
The binding specificity and affinity of the Tudor domains of TDRD3, SMN (zeige STMN1 Antikörper) and SPF30 (zeige SMNDC1 Antikörper) proteins were characterized quantitatively.
The TDRD3 is an effector molecule that promotes transcription by binding methylarginine marks on histone tails.
Tudor domain of TDRD3 was required for its recruitment to cytoplasmic stress granules.
propose a contribution of Tdrd3 to FMRP (zeige FMR1 Antikörper)-mediated translational repression and suggest that the loss of the FMRP (zeige FMR1 Antikörper)-Tdrd3 interaction caused by the I304N mutation might contribute to the pathogenesis of Fragile X (zeige FMR1 Antikörper) syndrome
Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine- methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins (By similarity).
tudor domain containing 3
, tudor domain-containing protein 3