Anti-HRD1

In 1X PBS, pH 7.4, with 0.09% sodium azide. HRD1 is a ubiquitin ligase whose expression is induced by the unfolded protein response (UPR) following endoplasmic reticulum stress. Expression of HRD1 protects cells from apoptosis by inducing degradation of abnormally processed proteins that accumulate in the endoplasmic reticulum. HRD1 is expressed in many tissues, strongly expressed in brain, pancreas, liver, kidney and skeletal muscle. Synoviolin/Hrd1 (expressed in rheumatoid synovium) is reported to be a novel causative factor for arthropathy by triggering synovial cell outgrowth through its antiapoptotic effects. HRD1 contains one ring-type zinc finger. Protein function: 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. [The UniProt Consortium]