Recombinant Mouse Hypoxia up-regulated protein 1 (Hyou1), partial

Product Details

Abbreviation
Hyou1
Purity
>85% (SDS-PAGE)
Target Names
Hyou1
Uniprot NO.
Alternative Names
Hyou1; Grp170; Hypoxia up-regulated protein 1; GRP-170; 140 kDa Ca(2+)-binding protein; CBP-140
Species
Mus musculus (Mouse)
Source
Yeast
Expression Region
33-999
Target Protein Sequence
LAVMSVDL GSESMKVAIV KPGVPMEIVL NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF QHLLGKQADN PHVALYRSRF PEHELIVDPQ RQTVRFQISP QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPAFF NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGSTVC TIVTYQTVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFDRVP GPVQQALQSA EMSLDQIEQV ILVGGATRVP KVQEVLLKAV GKEELGKNIN ADEAAAMGAV YQAAALSKAF KVKPFVVRDA VIYPILVEFT REVEEEPGLR SLKHNKRVLF SRMGPYPQRK VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA VQEEEESPAE GSKDEPAEQG ELKEEAEPPA EETSQPPPSE PKGDAAREGE KPDEKESGDK PEAQKPNEKG QAGPEGAAPA PEEDKKPKPA RKQKMVEEIG VELAVLDLPD LPEDELARSV QKLEELTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSATST WLEDEGFGAT TVMLKDKLAE LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR LIPEMDQVFT EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASAGDQEEK VIPPAGQTEE AKPILEPDKE ETGTEPADSE PLELGGPGAG PEQEEQSAGQ KRPSKNDEL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Partial
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.
Gene References into Functions
  1. The relative increase in ORP150 mRNA observed in hypoxia, compared with normoxia, may support its cytoprotective role in oxygendeprived conditions PMID:27748851
  2. 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. PMID:24327659
  3. 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. PMID:22892132
  4. Results reveal a previously unrecognized attribute of Grp170 as a superior DNA-binding chaperone capable of amplifying TLR9 activation on pathogen recognition. PMID:22207611
  5. AICAR infusion enhanced ORP150 expression, resulting in the marked amelioration of hepatic ER stress and apoptosis PMID:21296878
  6. 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. PMID:20210603
  7. 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. PMID:14674765
  8. demonstrated that expression of ORP150 in developing brain most likely serves a cytoprotective function in Purkinje cells PMID:14960622
  9. 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. PMID:15223375
  10. 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 PMID:15240565
  11. 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. PMID:15734840
  12. involvement of ORP150 in insulin secretion in MIN6 cells PMID:15841037
  13. 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 PMID:16424054
  14. 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. PMID:16849461
  15. 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. PMID:17330988
  16. Overexpression of ORP150 in mice leads to abetalipoproteinemia with alteration of glucose and lipid metabolism. PMID:17605339
  17. 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. PMID:18250584
  18. Grp170 enhances therapeutic activity of a novel tumor suppressor, mda-7/IL-24 PMID:18483274
  19. grp170 elicits systemic tumor immunity and may be used to improve treatment outcomes for prostate cancer. PMID:19142636

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Subcellular Location
Endoplasmic reticulum lumen.
Protein Families
Heat shock protein 70 family
Database Links
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No. 269, Shendun 5th Road, Donghu Hi-Tech Development Area, Hubei Province, 430206, P.R.China
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