Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Mouse (Murine) Anticorps:
anti-Rat (Rattus) Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Polyclonal DERL1 Primary Antibody pour IHC (fro), WB - ABIN540747
Schekman: Cell biology: a channel for protein waste. dans Nature 2004
Show all 2 Pubmed References
Chinese Hamster Polyclonal DERL1 Primary Antibody pour ICC, IF - ABIN151899
Huttunen, Guénette, Peach, Greco, Xia, Kim, Barren, Tanzi, Kovacs: HtrA2 regulates beta-amyloid precursor protein (APP) metabolism through endoplasmic reticulum-associated degradation. dans The Journal of biological chemistry 2007
Show all 2 Pubmed References
The derlin-1 pathway therefore may represent a significant early checkpoint in the recognition and degradation of ENaC in mammalian cells.
Cav-1 may be a cofactor in the interaction of Derlin-1 and N-glycosylated COX-2 and may facilitate Derlin-1- and p97 complex-mediated COX-2 ubiquitination, retrotranslocation, and degradation.
Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice
Derlin-1 regulates the turnover of superoxide dismutase 1 by promoting the proteasomal and autophagosomal degradation of SOD1 protein, but not by decreasing mutant SOD1 mRNA levels.
Perturbation of binding between SOD1(mut) and Derlin-1 by Derlin-1-derived oligopeptide suppressed SOD1(mut)-induced ER stress, ASK1 activation, and motor neuron death.
association of the degradation factor HRD1 with the translocon and the rerouting factor Derlin-1 may be necessary for the smooth and effective clearance of ERpQC substrates
Overexpression of Derlin-1 is Associated with Non-small Cell Lung Cancer.
These findings for the first time revealed that miR-598, as a tumor suppressor, negatively regulate DERL1 and Epithelial-Mesenchymal Transition to suppress the invasion and migration in Non-Small Cell Lung Cancer (NSCLC), thereby putatively serving as a novel therapeutic target for NSCLC clinical treatment.
ChIP assays were used to ascertain the correlations between HNF1beta and Derlin-1 in the miR-217/HNF1beta/Derlin-1 pathway in glioma cells
Derlin-1 is overexpressed in bladder cancer and promotes malignant phenotype through ERK/MMP-2/9 and PI3K/AKT signaling pathway.
Derlin-1 was overexpressed in bladder cancer and was associated with the malignancy of bladder cancer.
insights into the interactions between other SHP-containing proteins and p97N
data suggest that miR-181d is a tumor suppressor in ESCC inversely regulating its downstream target gene of DERL1.
Results showed that Derlin-1 is overexpressed in colon cancer and promotes proliferation of colon cancer cells.
TMEM129 contains an unusual cysteine-only RING with intrinsic E3 ligase activity and is recruited to US11 via Derlin-1.
Derlin-1 is overexpressed in non-small cell lung cancer and promotes invasion by EGFR-ERK-mediated up-regulation of MMP-2 and MMP-9.
Upregulation of derlin-1 may be associated with endoplasmic reticulum stress in neuronal cells in Alzheimer's disease.
These results indicate that ApoB after lipidation is dislocated from the ER lumen to the LD surface for proteasomal degradation and that Derlin-1 and UBXD8 are engaged in the predislocation and postdislocation steps, respectively.
Derlin-1 expression levels may affect glucose-stimulated insulin secretion by altering surface expression of K(ATP) channels.
Derlin-1 is a negative regulator for both glycosylated and non-glycosylated BCRP expression and provide a novel posttranslational regulatory mechanism of BCRP by Derlin-1.
Derlin-1 is an important factor for the extraction of certain aberrantly folded proteins from the mammalian ER
Derlin-1 interacts with US11, a virally encoded ER protein that specifically targets MHC class I heavy chains for export from the ER, as well as with VIMP, a novel membrane protein that recruits the p97 ATPase and its cofactor
Derlin-1 interacts with the N-terminal domain of PNGase via its cytosolic C-terminus. PNGase distributed in two populations; ER-associated and free in the cytosol, which suggests the deglycosylation process can proceed at either site
A role for DERL1 in tissue remodeling events and maintenance of function in reproductive tissues.
The protein encoded by this gene is a member of the derlin family. Members of this family participate in the ER-associated degradation response and retrotranslocate misfolded or unfolded proteins from the ER lumen to the cytosol for proteasomal degradation. This protein recognizes substrate in the ER and works in a complex to retrotranslocate it across the ER membrane into the cytosol. This protein may select cystic fibrosis transmembrane conductance regulator protein (CFTR) for degradation as well as unfolded proteins in Alzheimer's disease. Alternative splicing results in multiple transcript variants that encode different protein isoforms.
, Dm Derlin-1
, Der1-like domain family, member 1
, Der1-like protein 1
, degradation in endoplasmic reticulum protein 1
, der1-like protein 1