Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
The relative increase in ORP150 mRNA observed in hypoxia, compared with normoxia, may support its cytoprotective role in oxygendeprived conditions
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.
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 (show TGFB1 Proteins) and myofibroblasts.
Results reveal a previously unrecognized attribute of Grp170 as a superior DNA-binding chaperone capable of amplifying TLR9 (show TLR9 Proteins) activation on pathogen recognition.
AICAR (show ATIC Proteins) infusion enhanced ORP150 expression, resulting in the marked amelioration of hepatic ER stress and apoptosis
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.
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
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 (show GDF10 Proteins) and retrotranslocation.
Data reveal that Grp170 participates in preparing mutant proinsulin (show INS Proteins) for degradation while enabling wild-type proinsulin (show INS Proteins) escape from the endoplasmic reticulum.
High ORP150 expression is associated with thyroid cancer.
Two NEFs, Grp170 and Sil1 (show SIL1 Proteins), trigger toxin release from BiP (show GDF10 Proteins) to enable successful retrotranslocation and clarify the fate of the toxin after it disengages from BiP (show GDF10 Proteins).
Grp170 induces nucleotide exchange of BiP (show GDF10 Proteins) and releases SV40 virus from BiP (show GDF10 Proteins), promoting SV40 ER-to-cytosol transport and infection.
HYOU1 also modulates vIL (show VIL1 Proteins)-6's ability to induce CCL2 (show CCL2 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 (show SCNN1A Proteins).
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.
hypoxia up-regulated 1
, hypoxia up-regulated protein 1
, Hypoxia up-regulated protein 1
, hypoxia up-regulated protein 1-like
, 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
, 150 kDa oxygen-regulated protein
, oxygen regulated protein (150kD)
, 170 kDa glucose-regulated protein
, glucose-regulated protein 170
, glucose regulated protein, 170 kDa
, oxygen regulated protein, 150 kDa