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Chaperone specifically assisting the folding of beta- propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Zusätzlich bieten wir Ihnen MESDC2 Antikörper (47) und MESDC2 Proteine (11) und viele weitere Produktgruppen zu diesem Protein an.
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Mesd C-terminal region constitutes the major LRP5/6-binding domain, and that Mesd protein and its C-terminal region peptide have a potential therapeutic value in cancer
Results indicate that Mesd is a universal inhibitor of Wnt/LRP signaling on the cell surface.
Results provide evidence that MESD functions as a general LRP chaperone and suggest that the Mesd phenotype results from both signaling and endocytic defects resulting from misfolding of multiple LRP receptors.
Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/LRP6.
a high bone mass mutant LRP5(G171V), has subtly reduced Dkk1 binding, and, in contrast to LRP5, no enhancement of binding with MesD
as a result of (12;15)(q13;q25)translocation, the SUMO/Sentrin-specific protease 1 gene (SENP1) on chromosome 12 and the embryonic polarity-related mesoderm development gene (MESDC2) on chromosome 15 are disrupted and fused
Mesd and LRP6 modulate Wnt signaling.
Chaperone specifically assisting the folding of beta- propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway, since some LDLRs are coreceptors for the canonical Wnt pathway (By similarity).
mesoderm development candidate 2
, Mesoderm development candidate 2
, LDLR chaperone MESD
, mesoderm development protein
, renal carcinoma antigen NY-REN-61
, mesoderm development candiate 2