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Human Monoclonal HERPUD1 Primary Antibody for IHC (p), IP - ABIN564201
Lass, Kujawa, McConnell, Paton, Paton, Wójcik: Decreased ER-associated degradation of alpha-TCR induced by Grp78 depletion with the SubAB cytotoxin. in The international journal of biochemistry & cell biology 2008
Show all 3 Pubmed References
Human Polyclonal HERPUD1 Primary Antibody for ELISA, WB - ABIN564199
Hong, Kim, Kim, Lee, Shin, Son, Han, Sung, Kwon: Apoptosis induction of 2'-hydroxycinnamaldehyde as a proteasome inhibitor is associated with ER stress and mitochondrial perturbation in cancer cells. in Biochemical pharmacology 2007
This study showed that Herp stability was regulated by synoviolin through lysine ubiquitination-independent proteasomal degradation.
HERP plays an important role in the regulation of host innate immunity in response to ER stress during the infection of RNA viruses.
results indicated that low expression of miR-9-3p results in a high level of Herpud1, which may protect against apoptosis in glioma
Thus, our findings indicated that NQO1 could stabilize Herp protein expression via indirect regulation of synoviolin.
The authors found that the CREB3/Herp pathway limited the increase in cytosolic Ca2+ concentration and apoptosis early in poliovirus infection and this may reduce the extent of poliovirus-induced damage to the central nervous system during poliomyelitis.
HERPUD1 SNPs are highly associated with polypoidal choroidal vasculopathy.
concluded that the HERPUD1-mediated cytoprotective effect against oxidative stress depends on the ITPR and Ca(2+) transfer from the endoplasmic reticulum to mitochondria
The results indicate that Nrf1 is a transcriptional activator of Herpud1 expression during ER stress, and they suggest Nrf1 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 and MMP9 in tumor might be a valuable predictor for recurrence, especially for benign meningiomas
binding of Herp to Hrd1-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/p40) and IL-23 (p40/p19 heterodimers), and that this is associated with HERP function in the endoplasmic reticulum.
enhances presnilin-mediated generation of amyloid beta protein
upregulation by Wnt-1
may associate through its ubiquitin-like domain with the 26S proteasome, in this way connecting the protein degradation machinery to the ER membrane and resulting in an efficient ERAD
The ubiquitin-like domain of Herp most likely plays a role in the regulation of the intracellular level of Herp under ER stress
Results report the identification of Herp, a gene involved in ER stress-associated protein degradation (ERAD), as a direct target of Luman.
We identified the transcription factor binding site AARE (amino acid response element) by mutational analysis involved in Herp induction in SH-SY5Y cells, and the more significant role of the CREB binding site compared to AARE in HEK 293T cells.
that ERAD and proteasomal degradation were activated and that HERPUD1 expression was increased as osteoblast differentiation progressed
Herp deficiency inhibits the phenotypic switch of vascular smooth muscle cells and the development of atherosclerosis.
HERP depletion inhibits zearalenone-induced apoptosis of ovarian granulosa cells through autophagy activation and apoptotic pathway inhibition.
Herp is a newly identified huntingtin-interacting protein that is able to reduce the cytotoxicity of mutant huntingtin by inhibiting its aggregation and promoting its degradation.
Herpud1 is necessary for adequate insulin-induced glucose uptake due to its role in Ca(2+)/calcineurin regulation in L6 myotubes.
Herp may regulate the cell cycle and hormone secretions in mouse granulosa cells
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 knockout mice by attenuating inflammatory responses.
Data conclude that Herpud1 regulates insulin secretion via control of Nnt expression.
Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice
increased NADH levels resulting from ENOX2 inhibition result in decreased prosurvival sphingosine-1-phosphate and increased proapoptotic ceramide, both of which may be important to initiation of the ENOX2 inhibitor-induced apoptotic cascade.
Herp represents a second target, in addition to CHOP, 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, 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