Analytical Data
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Gene name
GPR78
- Application
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Alternative Names
GPR78；G-Protein coupled receptor 78
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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
Q96P69
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Expression Region
1-363aa
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AA Sequence
MGPGEALLAGLLVMVLAVALLSNALVLLCCAYSAELRTRASGVLLVNLSLGHLLLAALDMPFTLLGVMRGRTPSAPGACQVIGFLDTFLASNAALSVAALSADQWLAVGFPLRYAGRLRPRYAGLLLGCAWGQSLAFSGAALGCSWLGYSSAFASCSLRLPPEPERPRFAAFTATLHAVGFVLPLAVLCLTSLQVHRVARRHCQRMDTVTMKALALLADLHPSVRQRCLIQQKRRRHRATRKIGIAIATFLICFAPYVMTRLAELVPFVTVNAQWGILSKCLTYSKAVADPFTYSLLRRPFRQVLAGMVHRLLKRTPRPASTHDSSLDVAGMVHQLLKRTPRPASTHNGSVDTENDSCLQQTH
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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
GPR78, also known as G-protein-coupled receptor 78 or GRP78, is a prominent member of the heat shock protein 70 (HSP70) family, playing a crucial role in cellular stress responses and maintaining proteostasis. Its involvement in various physiological processes, such as cell survival, differentiation, and apoptosis, has garnered significant attention in biomedical research. Notably, GPR78 is implicated in the unfolded protein response (UPR), which is activated during endoplasmic reticulum (ER) stress. Research has shown that overexpression of GPR78 is associated with several diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, making it a potential therapeutic target. Furthermore, GPR78 has been linked to the development of drug resistance in cancer therapies, prompting studies to explore its role in mediating resistance mechanisms. The recombinant production of GPR78 protein is essential for elucidating its biological functions, understanding its structural properties, and developing targeted interventions to modulate its activity. Advances in recombinant DNA technology and protein expression systems have facilitated the generation of high-yield GPR78 proteins, enabling comprehensive investigations into its biochemical characteristics and interaction networks. This research not only enhances our understanding of GPR78's role in health and disease but also opens avenues for novel therapeutic strategies that exploit its unique properties as a critical regulator of cellular stress response pathways.
