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The protein encoded by DERL1 is a member of the derlin family. Additionally we are shipping Der1-Like Domain Family, Member 1 Antibodies (66) and many more products for this protein.
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Cav-1 (show CAV1 Proteins) may be a cofactor in the interaction of Derlin-1 and N-glycosylated COX-2 and may facilitate Derlin-1- and p97 (show EIF4G2 Proteins) complex-mediated COX-2 ubiquitination, retrotranslocation, and degradation.
Derlin-1 deficiency is embryonic lethal, Derlin-3 (show DERL3 Proteins) deficiency appears normal, and Herp (show HERPUD1 Proteins) deficiency is intolerant to glucose load and ischemia in mice
Derlin-1 regulates the turnover of superoxide dismutase 1 (show SOD1 Proteins) by promoting the proteasomal and autophagosomal degradation of SOD1 (show SOD1 Proteins) protein, but not by decreasing mutant SOD1 (show SOD1 Proteins) mRNA levels.
Perturbation of binding between SOD1 (show SOD1 Proteins)(mut (show MUT Proteins)) and Derlin-1 by Derlin-1-derived oligopeptide suppressed SOD1 (show SOD1 Proteins)(mut (show MUT Proteins))-induced ER stress, ASK1 (show MAP3K5 Proteins) activation, and motor neuron death.
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 (show EGFR Proteins)-ERK (show EPHB2 Proteins)-mediated up-regulation of MMP-2 (show MMP2 Proteins) and MMP-9 (show MMP9 Proteins).
Upregulation of derlin-1 may be associated with endoplasmic reticulum stress in neuronal cells in Alzheimer's disease.
These results indicate that ApoB (show APOB Proteins) after lipidation is dislocated from the ER lumen to the LD surface for proteasomal degradation and that Derlin-1 and UBXD8 (show FAF2 Proteins) are engaged in the predislocation and postdislocation steps, respectively.
Derlin-1 expression levels may affect glucose-stimulated insulin (show INS Proteins) 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 (show SELS Proteins), a novel membrane protein that recruits the p97 ATPase (show vcp Proteins) and its cofactor
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