Analytical Data
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Gene name
S1PR5
- Application
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Alternative Names
S1PR5
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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
Q9H228
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Expression Region
309-398 aa
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AA Sequence
TNRDLRHALLRLVCCGRHSCGRDPSGSQQSASAAEASGGLRRCLPPGLDGSFSGSERSSPQRDGLDTSGSTGSPGAPTAARTLVSEPAAD
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Molecular Weight
16 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
S1PR5, or sphingosine-1-phosphate receptor 5, is a G-protein-coupled receptor that plays a crucial role in various physiological processes, including immune regulation, cell migration, and vascular development. Its unique ability to mediate signaling by the bioactive lipid sphingosine-1-phosphate (S1P) has garnered significant interest in understanding its implications in health and disease. Recent research has highlighted S1PR5's involvement in the progression of autoimmune diseases, cancers, and neurodegenerative disorders, making it a potential therapeutic target. The study of S1PR5 recombinant proteins has become essential for elucidating the receptor's function, interactions, and signaling pathways. By producing and characterizing these recombinant proteins, researchers can investigate the molecular mechanisms underlying S1PR5-mediated signaling and explore its role in cellular responses. Furthermore, S1PR5's potential as a drug target has prompted the development of small molecules and antibodies that can modulate its activity, paving the way for novel treatment strategies. Understanding the structure and function of S1PR5 through recombinant protein studies is thus critical for advancing therapeutic interventions in diseases associated with dysregulated sphingosine-1-phosphate signaling.
