ab172730 - Rabbit monoclonal IgG, is suitable for use as an isotype control with this antibody.
1/10 - 1/100.
Is unsuitable for IHC-P.
Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis.
Ubiquitously expressed, with highest levels in liver and kidney (at protein level). Up-regulated in synovial tissues from patients with rheumatoid arthritis (at protein level).
Protein modification; protein ubiquitination.
Belongs to the HRD1 family. Contains 1 RING-type zinc finger.
The RING-type zinc finger is required for E3 ligase activity.
Feng L et al. Ubiquitin ligase SYVN1/HRD1 facilitates degradation of the SERPINA1 Z variant/a-1-antitrypsin Z variant via SQSTM1/p62-dependent selective autophagy. Autophagy13:686-702 (2017).
Read more (PubMed: 28121484) »
Kong S et al. Endoplasmic reticulum-resident E3 ubiquitin ligase Hrd1 controls B-cell immunity through degradation of the death receptor CD95/Fas. Proc Natl Acad Sci U S A113:10394-9 (2016).
Read more (PubMed: 27573825) »