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

Code CSB-YP862399MO
MSDS
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Source Yeast
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Code CSB-EP862399MO
MSDS
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Source E.coli
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Code CSB-EP862399MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP862399MO
MSDS
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Source Baculovirus
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Code CSB-MP862399MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
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)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
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.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
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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