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Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity.
[Protein ADP-ribosylaspartate] hydrolase MACROD1; [Protein ADP-ribosylglutamate] hydrolase; [Protein ADP-ribosylglutamate] hydrolase MACROD1; ADP-ribose glycohydrolase MACROD1; ADP-ribose glycohydrolase MACROD1; O-acetyl-ADP-ribose deacetylase MACROD1; AI604841; AW743046; D930010J01Rik; LOC613568 protein; Lrp16; MACRO domain containing 1; MACRO domain-containing protein 1; MACROD1; mono-ADP ribosylhydrolase 1; O-acetyl-ADP-ribose deacetylase MACROD1; O-acetyl-ADP-ribose deacetylase MACROD1; LOW QUALITY PROTEIN: O-acetyl-ADP-ribose deacetylase MACROD1; Protein LRP16
100 µg
100 µL
100 µL
100 µL
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