Analytical Data
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Gene name
SSTR5
- Application
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Alternative Names
SSTR5；Somatostatin receptor type 5
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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
P35346
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Expression Region
307-364aa
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AA Sequence
LSDNFRQSFQKVLCLRKGSGAKDADATEPRPDRIRQQQEATPPAHRAAANGLMQTSKL
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Molecular Weight
8.0 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
Related Products
Protein Description
SSTR5, or somatostatin receptor type 5, is a G-protein coupled receptor that plays a crucial role in the regulation of various physiological processes, including hormone secretion, neurotransmission, and cellular proliferation. It is primarily expressed in the brain, pancreas, and gastrointestinal tract, and is known for its significant function in inhibiting the release of multiple hormones. The study of SSTR5 is particularly important in the context of neuroendocrine tumors and conditions like acromegaly, where its signaling pathways may be dysregulated. Recombinant SSTR5 proteins have garnered attention in research due to their potential application in targeted therapies and diagnostics. By creating and studying these recombinant proteins, researchers aim to better understand the receptor's structure, function, and interaction with ligands. This knowledge could facilitate the development of SSTR5-targeted treatments that improve patient outcomes in neuroendocrine malignancies. Furthermore, advancements in recombinant DNA technology have enabled scientists to produce functional SSTR5 with high purity and activity, allowing for detailed biochemical and pharmacological studies. As a result, research on SSTR5 recombinant proteins is paving the way for novel therapeutic strategies and enhancing our understanding of complex neuroendocrine signaling mechanisms.
