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DPY30 is a component of a Set1-like multiprotein histone methyltransferase complex (Cho et al., 2007 [PubMed 17500065]).[supplied by OMIM, May 2008].. De plus, nous expédions DPY30 Anticorps (11) et beaucoup plus de produits pour cette protéine.
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The PKA-binding domain of AKAP8 and the C-terminal domain of DPY30, also called Dpy-30 motif, are crucial for the interaction between these proteins. A single amino acid substitution in DPY30 L69D affects its dimerization and completely abolishes its interaction with AKAP8 and BIG1.
Dpy30 role in cellular reprogramming and its interactions with Set1 complex
results indicate that DPY30 has critical roles in the proliferation, migration, and invasion of gastric cancer cells, and suggest DPY30 might be a therapeutic target in gastric cancer
Based on our structural data and cross-linking results, we suggest that Dpy30 may regulate H3K4 methylation according to its copy number in COMPASS
these results form the basis for understanding how WRAD(DRY-30) differentially regulates SET1 family complexes in vivo.
The DPY30 subunit in SET1/MLL complexes regulates the proliferation and differentiation of hematopoietic progenitor cells.
A deletion mutation and reduced DPY30 expression in a Spastic Paraplegia type 4 Japanese family.
DPY30 regulates pathways in cellular senescence through ID protein expression.
determination of the minimum motif of Ash2L that is required for DPY30 interaction; a structural model for the Ash2L-DPY30 interaction
First report of SPG4 associated with partial deletions of both the SPAST and DPY30 genes. The partial heterozygous deletion of DPY30 could modify the phenotypic expression of SPG4 patients with this pedigree.
The DPY-30 C-terminal domain structure, harboring the conserved DPY-30 motif, is composed of two alpha-helices linked by a sharp loop and forms a typical X-type four-helix bundle required for dimer formation.
hDPY-30 (dpy-30-like protein) binds ASH2L directly. The evolutionarily conserved hDPY-30, ASH2L, RBBP5 and WDR5 likely constitute a subcomplex that is shared by all human Set1-like HMT complexes.
Dpy30-deficient hematopoietic stem and progenitor cells cannot differentiate or efficiently up-regulate lineage-regulatory genes, and eventually fail to sustain for long term.
Results indicate an essential functional role for Dpy-30 and SET1/MLL complex-mediated H3K4 methylation, as a component of the bivalent mark, at developmental genes during the embryonic stem cells fate transitions.
DPY30 is a component of a Set1-like multiprotein histone methyltransferase complex (Cho et al., 2007
, protein dpy-30 homolog
, dosage compensation-related protein DPY30
, protein rAIP1