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The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the ER stress response. Additionally we are shipping Homocysteine-Inducible, Endoplasmic Reticulum Stress-Inducible, Ubiquitin-Like Domain Member 1 Antibodies (67) and Homocysteine-Inducible, Endoplasmic Reticulum Stress-Inducible, Ubiquitin-Like Domain Member 1 Kits (4) and many more products for this protein.
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concluded that the HERPUD1-mediated cytoprotective effect against oxidative stress depends on the ITPR and Ca(2 (show CA2 Proteins)+) transfer from the endoplasmic reticulum to mitochondria
The results indicate that Nrf1 (show NFE2L1 Proteins) is a transcriptional activator of Herpud1 expression during ER stress, and they suggest Nrf1 (show NFE2L1 Proteins) is a key player in the regulation of the ER stress response in cells.
Herp operates as a relevant factor in the defense against glucose starvation by modulating autophagy levels.
Together with histological grade, increased co-expression of MIF (show AMH Proteins) and MMP9 (show MMP9 Proteins) in tumor might be a valuable predictor for recurrence, especially for benign meningiomas
binding of Herp to Hrd1 (show SYVN1 Proteins)-containing ERAD complexes positively regulates the ubiquitylation activity of these complexes, thus permitting survival of the cell during ER stress.
The results suggest that ERAD molecule Herp may delay the degradation of cytosolic proteins at the ubiquitination step.
Herp mimics structural determinants of DNA immunologically and can be immunogenic in vivo. Thus, Herp represents a candidate autoantigen for anti-DNA antibodies.
Data show that that 4-trifluoromethyl-celecoxib can inhibit secretion but not transcription of IL-12 (p35 (show IL12A Proteins)/p40 (show IL9 Proteins)) and IL-23 (p40/p19 (show CDKN2D Proteins) heterodimers), and that this is associated with HERP function in the endoplasmic reticulum.
upregulation by Wnt-1 (show WNT1 Proteins)
may associate through its ubiquitin-like domain with the 26S proteasome (show Psmd4 Proteins), in this way connecting the protein degradation machinery to the ER membrane and resulting in an efficient ERAD
Herp lentiviral shRNA vectors had been successfully constructed; knockdown Herp inhibited ER stress and had a different effect on inflammatory responses in RAW 264.7 macrophages depending on whether they were exposed to tunicamycin or thapsigargin
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.
A deficiency of Herp, an endoplasmic reticulum stress protein, suppresses atherosclerosis in ApoE (show APOE Proteins) knockout mice by attenuating inflammatory responses.
Data conclude that Herpud1 regulates insulin (show INS Proteins) secretion via control of Nnt (show NNT Proteins) expression.
Derlin-1 (show DERL1 Proteins) deficiency is embryonic lethal, Derlin-3 (show DERL3 Proteins) deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice
increased NADH levels resulting from ENOX2 (show ENOX2 Proteins) inhibition result in decreased prosurvival sphingosine-1-phosphate and increased proapoptotic ceramide, both of which may be important to initiation of the ENOX2 (show ENOX2 Proteins) inhibitor-induced apoptotic cascade.
Herp represents a second target, in addition to CHOP (show DDIT3 Proteins), that is dually regulated by both the shared and the ER stress-specific branches during unfolded protein activation
Herp is in a complex with ubiquitinated proteins and with the 26S proteasome (show Psmd4 Proteins), suggesting that it plays a role in linking substrates with the proteasome.
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the ER stress response. This response includes the inhibition of translation to prevent further accumulation of unfolded proteins, the increased expression of proteins involved in polypeptide folding, known as the unfolded protein response (UPR), and the destruction of misfolded proteins by the ER-associated protein degradation (ERAD) system. This gene may play a role in both UPR and ERAD. Its expression is induced by UPR and it has an ER stress response element in its promoter region while the encoded protein has an N-terminal ubiquitin-like domain which may interact with the ERAD system. This protein has been shown to interact with presenilin proteins and to increase the level of amyloid-beta protein following its overexpression. Alternative splicing of this gene produces multiple transcript variants encoding different isoforms. The full-length nature of all transcript variants has not been determined.
homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1
, homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein
, homocysteine-inducible endoplasmic reticulum stress-inducible ubiquitin-like domain member 1 protein
, methyl methanesulfonate (MMF)-inducible fragment protein 1