Analytical Data
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Gene name
SSTR2
- Application
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Alternative Names
SSTR2; somatostatin receptor 2; somatostatin receptor type 2; SS2R; SRIF-1; SS-2-R
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Species
Human
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30874
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Expression Region
M1-I369
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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
SSTR2, or Somatostatin Receptor Type 2, is a G-protein-coupled receptor that plays a crucial role in various physiological processes, including the regulation of endocrine functions and neuroendocrine tumors. The research surrounding SSTR2 has gained significant attention due to its implications in cancer biology, particularly in neuroendocrine tumors where it is often overexpressed. This receptor is a primary target for somatostatin analogs, which are used in both diagnostic imaging and therapeutic applications for conditions like acromegaly and carcinoid syndrome. The characterization of SSTR2 recombinant proteins is vital for understanding its structure-function relationship, signaling pathways, and interactions with potential therapeutic agents. By producing and purifying these recombinant proteins, researchers can investigate various aspects, such as receptor-ligand binding, cellular signaling mechanisms, and the development of novel therapeutics. This research not only enhances our understanding of SSTR2's role in normal physiology but also aids in the development of targeted therapies for SSTR2-expressing tumors. As such, ongoing studies focus on optimizing the expression and purification methods of SSTR2 recombinant proteins to facilitate structural and functional analyses, ultimately contributing to the advancement of precision medicine strategies in oncology.
