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anti-Human HYOU1 Antibodies:
anti-Mouse (Murine) HYOU1 Antibodies:
anti-Rat (Rattus) HYOU1 Antibodies:
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Human Monoclonal HYOU1 Primary Antibody for IHC (p), ELISA - ABIN564589
Liu, Li, Bai, Zhang, Tang, Lei, Chen, Liang, Zhao, Wei, Huang: Mechanism of cancer cell adaptation to metabolic stress: proteomics identification of a novel thyroid hormone-mediated gastric carcinogenic signaling pathway. in Molecular & cellular proteomics : MCP 2009
Show all 3 Pubmed References
Human Polyclonal HYOU1 Primary Antibody for IF (p), IHC (p) - ABIN705851
Ruan, Huang, Jin, Chen, Li, Gong: Tetrandrine attenuated cerebral ischemia/reperfusion injury and induced differential proteomic changes in a MCAO mice model using 2-D DIGE. in Neurochemical research 2013
Cow (Bovine) Polyclonal HYOU1 Primary Antibody for WB - ABIN2782712
Du, Rong, Hui, Peng, Jin, Li, Wang, Li: Expression and function of HSP110 family in mouse testis after vasectomy. in Asian journal of andrology 2016
ORP150 and CHIP demonstrate antagonism under normal and stress conditions wherein they inversely regulate each other thus affecting BACE1 level.
These results strongly suggest that AMPK can activate ORP150 through FOXO1 pathway and confer protection against endoplasmic reticulum stress - induced apoptosis of airway epithelial cells following exposure to cigarette smoke extract.
Findings establish a general function of Grp170 during ERAD and suggest that positioning this client-release factor at the retrotranslocation site may afford a mechanism to couple client release from BiP and retrotranslocation.
Data reveal that Grp170 participates in preparing mutant proinsulin for degradation while enabling wild-type proinsulin escape from the endoplasmic reticulum.
High ORP150 expression is associated with thyroid cancer.
Two NEFs, Grp170 and Sil1, trigger toxin release from BiP to enable successful retrotranslocation and clarify the fate of the toxin after it disengages from BiP.
Grp170 induces nucleotide exchange of BiP and releases SV40 virus from BiP, promoting SV40 ER-to-cytosol transport and infection.
HYOU1 also modulates vIL-6's ability to induce CCL2.
Here we show that Grp170 can bind directly to a variety of incompletely folded protein substrates in the endoplasmic reticulum, and as expected for a bona fide chaperone, it does not interact with folded secretory proteins.
inducible overexpression of ORP150, in ER stress conditions, exerts inhibitory effect on apoptosis and senescence in human breast carcinoma cells but not in normal fibroblasts
Data indicate that Grp170 (Lhs1 ortholog) coprecipitate with alphaENaC.
AICAR infusion enhanced ORP150 expression, resulting in the marked amelioration of hepatic ER stress and apoptosis
Report ORP-150 levels in autopsy tissue after hypoxia/ischemia events in term neonates.
ORP150 exerts cytoprotective effects in renal tubular epithelia subjected to I/R injury and suggest a key role for ER stress in the renal tubular response to acute renal failure
Hypoxia results in an enhancement of ORP 150 expression in several tumour cell lines.
These findings suggest that ORP150 is structurally and functionally well conserved in distant species
Our observations led to the hypothesis that ORP150 protects against MPTP/MPP(+)-induced neurotoxicity, and indicate the importance of the ER environment in maintaining the nigrostriatal pathways.
data indicate ORP150 inhibits oxLDL-induced apoptosis by blocking calcium signaling & apoptosis; calcium released from ER stores is inhibited by ORP150; ORP150 is expressed in advanced atherosclerotic lesions
The forced expression of ORP150 highlights its new protective role against oxLDL-induced ER stress and subsequent apoptosis
the increased expression of ORP150 is a factor which protects collagen against intracellular degradation induced by glucose deprivation.
The relative increase in ORP150 mRNA observed in hypoxia, compared with normoxia, may support its cytoprotective role in oxygendeprived conditions
These results suggest that although ORP150 is protective against bleomycin-induced lung injury, this protein could stimulate bleomycin-induced pulmonary fibrosis by increasing pulmonary levels of TGF-beta1 and myofibroblasts.
Results reveal a previously unrecognized attribute of Grp170 as a superior DNA-binding chaperone capable of amplifying TLR9 activation on pathogen recognition.
Secreted grp170 can bind to and co-transport out of tumour cells a full length tumour antigen that may play a role in the anti-tumour immune response.
Grp170 displays multiple peptide binding domains; the presence of two strong peptide binding regions in such a large protein may facilitate the interactions and assembly of two substate proteins.
demonstrated that expression of ORP150 in developing brain most likely serves a cytoprotective function in Purkinje cells
The 150-kDa oxygen-regulated protein may be cytoprotective against ischemia/reperfusion injury via reduction of endoplasmic reticulum stress and probably also inhibition of apoptosis.
Systemic expression of ORP150 in Akita mice improves insulin intolerance, whereas the exclusive overexpression of ORP150 in pancreatic beta-cells of Akita mice did not change their glucose tolerance.
involvement of ORP150 in insulin secretion in MIN6 cells
molecular chaperoning is involved in stress protein interactions with APCs, antigen binding, and in eliciting antitumor immunity, thus bridging this ancient function of stress proteins in prokaryotes to their ability to elicit immunity in higher organisms
Grp170 depleted of endoplasmic reticulum retention sequence "KNDEL," when secreted by B16 melanoma cells, maintains its highly efficient chaperoning activities and is significantly superior to both hsp70 and gp96.
Overexpression of ORP150 in mice leads to abetalipoproteinemia with alteration of glucose and lipid metabolism.
These findings suggest that overexpression of ORP150 causes accumulation of ORP150 in the rough-surfaced endoplasmic reticula, resulting in vacuolar degeneration in the skeletal muscle of ORP-Tg mice.
Grp170 enhances therapeutic activity of a novel tumor suppressor, mda-7/IL-24
grp170 elicits systemic tumor immunity and may be used to improve treatment outcomes for prostate cancer.
The protein encoded by this gene belongs to the heat shock protein 70 family. This gene uses alternative transcription start sites. A cis-acting segment found in the 5' UTR is involved in stress-dependent induction, resulting in the accumulation of this protein in the endoplasmic reticulum (ER) under hypoxic conditions. The protein encoded by this gene is thought to play an important role in protein folding and secretion in the ER. Since suppression of the protein is associated with accelerated apoptosis, it is also suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness. This gene also has an alternative translation initiation site, resulting in a protein that lacks the N-terminal signal peptide. This signal peptide-lacking protein, which is only 3 amino acids shorter than the mature protein in the ER, is thought to have a housekeeping function in the cytosol. In rat, this protein localizes to both the ER by a carboxy-terminal peptide sequence and to mitochondria by an amino-terminal targeting signal.
150 kDa oxygen-regulated protein
, 170 kDa glucose-regulated protein
, glucose-regulated protein 170
, hypoxia up-regulated protein 1
, oxygen regulated protein (150kD)
, 140 kDa Ca(2+)-binding protein
, 150-kDa oxygen regulated protein
, 170 kDa glucose regulated protein GRP170
, calcium binding protein 140
, calcium binding protein, 140 kDa
, hypoxia up-regulated 1
, Hypoxia up-regulated protein 1
, hypoxia up-regulated protein 1-like
, glucose regulated protein, 170 kDa
, oxygen regulated protein, 150 kDa