Analytical Data
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Gene name
HYOU1
- Application
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Alternative Names
HYOU1；GRP170；HSPH4；ORP150；Hypoxia up-regulated Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y4L1
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Expression Region
695-994aa
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AA Sequence
MVEEIGVELVVLDLPDLPEDKLAQSVQKLQDLTLRDLEKQEREKAANSLEAFIFETQDKLYQPEYQEVSTEEQREEISGKLSAASTWLEDEGVGATTVMLKEKLAELRKLCQGLFFRVEERKKWPERLSALDNLLNHSSMFLKGARLIPEMDQIFTEVEMTTLEKVINETWAWKNATLAEQAKLPATEKPVLLSKDIEAKMMALDREVQYLLNKAKFTKPRPRPKDKNGTRAEPPLNASASDQGEKVIPPAGQTEDAEPISEPEKVETGSEPGDTEPLELGGPGAEPEQKEQSTGQKRPL
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Molecular Weight
37.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
HYOU1, also known as hypoxia-upregulated 1, is a protein that plays a pivotal role in cellular responses to hypoxic stress, which is a condition where there is insufficient oxygen supply. This protein is primarily involved in the endoplasmic reticulum (ER) stress response and the regulation of protein folding, ensuring proper cellular function under stress conditions. The study of HYOU1 has gained significant traction due to its potential implications in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Under hypoxic conditions, HYOU1 expression is upregulated, suggesting its involvement in adaptive mechanisms that protect cells from damage. Moreover, its role in modulating the unfolded protein response (UPR) indicates its importance in maintaining cellular homeostasis. Recent research has focused on the potential of HYOU1 as a biomarker for disease diagnosis and prognosis, as well as its possible therapeutic targets in modulating stress responses in diseased tissues. Understanding the molecular mechanisms underlying HYOU1's function could provide insights into its role in disease progression and open avenues for innovative treatment strategies. As the study of HYOU1 continues to evolve, it presents an intriguing intersection of basic biological research and clinical application, with the aim of translating its findings into effective therapeutic interventions.
