Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P30874 |
express system | HEK293 |
product tag | |
purity | > 95% as determined by HPLC |
background | Somatostatin receptor (SSTR) 2, widely expressed in meningioma, is a G-protein-coupled receptor and can be activated by somatostatin or its synthetic analogs. SSTR2 is therefore extensively studied as a marker and target for the diagnosis and treatment of meningioma. |
molecular weight | The target protein has a predicted MW of 42.7 kDa. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human SSTR2 Protein-VLP 3312
$1,100.00 – $3,800.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Met1-Ile369
Human SSTR2 Protein-VLP 3312
protein |
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Size and concentration 100, 500µg and liquid |
Form Liquid |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped with dry ice. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Somatostatin receptor (SSTR) 2, widely expressed in meningioma, is a G-protein-coupled receptor and can be activated by somatostatin or its synthetic analogs. SSTR2 is therefore extensively studied as a marker and target for the diagnosis and treatment of meningioma. |
Protein names Somatostatin receptor type 2 (SS-2-R) (SS2-R) (SS2R) (SST2) (SRIF-1) |
Gene names SSTR2,SSTR2 |
Protein family G-protein coupled receptor 1 family |
Mass 9606Da |
Function Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization. |
Subellular location Cell membrane; Multi-pass membrane protein. Cytoplasm. Note=Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm. |
Tissues Expressed in both pancreatic alpha- and beta-cells (at protein level). Expressed at higher levels in the pancreas than other somatostatin receptors. Also expressed in the cerebrum and kidney and, in lesser amounts, in the jejunum, colon and liver. In the developing nervous system, expressed in the cortex where it is located in the preplate at early stages and is enriched in the outer part of the germinal zone at later stages. In the cerebellum, expressed in the deep part of the external granular layer at gestational week 19. This pattern persists until birth but disappears at adulthood. |
Structure Homodimer and heterodimer with SSTR3 and SSTR5. Heterodimerization with SSTR3 inactivates SSTR3 receptor function. Heterodimerization with SSTR5 is enhanced by agonist stimulation of SSTR2 and increases SSTR2 cell growth inhibition activity. Following agonist stimulation, homodimers dissociate into monomers which is required for receptor internalization. Interacts with beta-arrestin; this interaction is necessary for receptor internalization and is destabilized by heterodimerization with SSTR5 which results in increased recycling of SSTR2 to the cell surface. Interacts (via C-terminus) with SHANK1 (via PDZ domain). |
Post-translational modification Phosphorylated on serine and threonine residues in response to agonist stimulation, leading to receptor desensitization and rapid internalization. Phosphorylated to a greater extent on serine than threonine residues. Threonine phosphorylation is required for arrestin binding and receptor endocytosis but is not necessary for desensitization (By similarity). |
Target Relevance information above includes information from UniProt accession: P30874 |
The UniProt Consortium |
Data
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
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Protocols
relevant to this product |
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Documents
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