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SYVN1 encodes a protein involved in endoplasmic reticulum (ER)-associated degradation. Additionally we are shipping Synovial Apoptosis Inhibitor 1, Synoviolin Antibodies (101) and Synovial Apoptosis Inhibitor 1, Synoviolin Kits (3) and many more products for this protein.
Showing 6 out of 7 products:
Prion protein (show PRNP Proteins) mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP (show GDF10 Proteins).
OS-9 (show OS9 Proteins), an ER-resident lectin, acts downstream of Grp94 (show HSP90B1 Proteins) to further recognize misfolded alpha1 subunits in a glycan-dependent manner. This delivers misfolded alpha1 subunits to the Hrd1-mediated ubiquitination and the valosin-containing protein (show vcp Proteins)-mediated extraction pathway.
These findings uncover a novel role for HRD1 in breast cancer.
The inherently unstable nature of the human SEL1L (show SEL1L Proteins) protein lies in its transmembrane domain, and that association of HRD1 with the SEL1L (show SEL1L Proteins) transmembrane domain restored its stability.
specific silencing of Derlin-2 (show DERL2 Proteins), p97 (show EIF4G2 Proteins) and HRD1 by shRNAs increases steady state levels of proinsulin (show INS Proteins). these ERAD constituents are critically involved in proinsulin (show INS Proteins) degradation and may therefore also play a role in subsequent antigen generation.
Charcot-Marie-Tooth disease-related PMP22 (show PMP22 Proteins) is trapped in the endoplasmic reticulum by calnexin (show CANX Proteins)-dependent retention and Rer1 (show RER1 Proteins)-mediated early Golgi retrieval systems and partly degraded by the Hrd1-mediated endoplasmic reticulum-associated degradation system.
Results show that HRD1 and RFP2 (show TRIM13 Proteins) contributes are required for the disposal of V247M alpha-sarcoglycan (show SGCA Proteins) mutant.
Herp localizes to the endoplasmic reticulum-derived quality control compartment (ERQC) and recruits HRD1, which targets to endoplasmic reticulum associated degradation the substrate presented by the OS-9 lectin at the ERQC.
HRD1 and RMA1 may therefore be negative regulators of disease-associated transporter ABCG5 (show ABCG5 Proteins)/ABCG8 (show ABCG8 Proteins).
identified Hrd1 as a novel E3 ubiquitin ligase (show MUL1 Proteins) responsible for compromised Nrf2 (show GABPA Proteins) response during liver cirrhosis
SYVN1 may play an important role in inhibiting ER stress, chronic inflammation, and vascular overgrowth associated with DR.
Data show that inositol requiring enzyme 1alpha (IRE1alpha (show ERN1 Proteins)), the sensor of the unfolded protein response (UPR), is a bona fide substrate of the Sel1L (show SEL1L Proteins) proten-Hrd1 protein endoplasmic reticulum (ER)-associated degradation (ERAD) complex.
Hrd1 is an essential component of the adaptive endoplasmic reticulum stress response in cardiac myocytes.
The results highlight a novel function for SYVN1 in the control of body weight and mitochondrial biogenesis through negative regulation of PGC (show PGC Proteins)-1b.
Data indicate that E3 ubiquitin-protein ligase (show UBE2K Proteins) Hrd1 catalyzed ubiquitination and degradation of the transcriptional suppressor B lymphocyte-induced maturation protein 1 (BLIMP1 (show PRDM1 Proteins)) to promote MHC-II antigen expression.
oxidative stress-induced (show SQSTM1 Proteins) HRD1 insolubilization might be involved in a vicious cycle of increased amyloid beta production and amyloid beta-induced oxidative stress in Alzheimer's disease pathogenesis.
results indicate that Hrd1 plays an important role in the maturation of collagen I in renal fibrosis, and that Sec23A (show SEC23A Proteins) pathway is required for ER-to-Golgi procollagen trafficking to promote collagen synthesis
Synoviolin up-regulates amyloid beta production by targeting a negative regulator of gamma-secretase, Rer1 (show RER1 Proteins), for degradation.
HRD1 is colocated with the neural stem cell marker protein nestin (show NES Proteins) and glial fibrillary acidic protein (show GFAP Proteins) in the endoplasmic reticulum membrane of the NSCs of the subventricular zone (SVZ astrocytes) but in the cell nucleus of in the dentate gyrus
these results clearly suggest that both beta-TrCP (show BTRC Proteins)- and Hrd1-dependent degradation mechanisms regulate the transcriptional activity of Nrf1 (show NRF1 Proteins) to maintain cellular homeostasis.
This gene encodes a protein involved in endoplasmic reticulum (ER)-associated degradation. The encoded protein removes unfolded proteins, accumulated during ER stress, by retrograde transport to the cytosol from the ER. This protein also uses the ubiquitin-proteasome system for additional degradation of unfolded proteins. Sequence analysis identified two transcript variants that encode different isoforms.
E3 ubiquitin-protein ligase synoviolin
, synovial apoptosis inhibitor 1, synoviolin
, HMG-coA reductase degradation 1 homolog
, synoviolin 1
, HRD1 protein