SSTR2 Antibodies

Background

SSTR2 (somatostatin receptor 2) is a G protein-coupled receptor that is mainly distributed on the surface of neuroendocrine cells and various tumor cells. This receptor regulates physiological processes such as cell proliferation, hormone secretion and signal transduction by specifically binding to somatostatin peptide hormones. Medical research particularly focuses on the high expression characteristics of SSTR2 in neuroendocrine tumors, making it a key biomarker for molecular imaging diagnosis and targeted radiotherapy. Since its clonal identification in the early 1990s, novel tracers and radioligand therapies targeting this receptor have been successfully applied in clinical practice, promoting the development of precision oncology. Its unique transmembrane domain and ligand binding mechanism continuously provide important models for the development of GPCR-targeted drugs, profoundly influencing the innovation of cell signal regulation theory and therapeutic strategies.

Structure Function Application Advantage Our Products

Structure of SSTR2

The molecular weight of the protein encoded by the SSTR2 gene is approximately 41.5 kDa, and this value may fluctuate slightly among different species due to differences in the degree of glycosylation and amino acid composition.

Species	Human	Mouse	Rat	Monkey
Molecular Weight (kDa)	~41.5	~40.8	~41.2	~41.5
Primary Structural Differences	Contains seven transmembrane domain structure, n-terminal outside the cell	Across the membrane area highly conservative, inner ring of the cytoplasm area have small differences	Highly homologous ligand binding pocket	More than 95% homology to the human receptor

This receptor belongs to the classic superfamily of seven-time transmembrane G protein-coupled receptors, and its primary structure contains approximately 369 amino acid residues. The core of its three-dimensional conformation is seven α -helices (TM1-TM7) spanning the cell membrane, which together form a ligand-binding pocket. The key structural features include a conserved binding cavity composed of multiple aromatic amino acids, as well as a specific sequence on the intracellular third loop responsible for coupling with Gi/o proteins. Its N-terminal is located outside the cell and has a glycosylation site, while the C-terminal is located in the cytoplasm and contains serine/threonine residues that can be phosphorylated. These structures jointly determine the ligand specificity, membrane localization and signal transduction function of the receptor.

Fig. 1 The cryo-EM structure of SSTR2–DNGi complex.¹

Key structural properties of SSTR2:

Seven-time transmembrane helical structure
Conservative ligand-binding pocket
Intracellular signal transduction module

Functions of SSTR2

The main function of the SSTR2 gene is to mediate the signal transduction of somatostatin, regulate cell proliferation and endocrine balance. In addition, it is also involved in a wide range of physiological and pathological processes such as tumor suppression, immune regulation and metabolic homeostasis.

Function	Description
Hormone secretion inhibition	By inhibiting adenylate cyclase through Gi/o protein coupling, the intracellular cAMP level is reduced, thereby suppressing the secretion of various hormones such as growth hormone, insulin, and glucagon.
Cell Proliferation Regulation	Activate downstream pathways such as tyrosine phosphatase and MAPK, induce cell cycle arrest at the G1 phase, and inhibit the proliferation of neuroendocrine cells and various tumor cells.
Tumor Targeted Diagnosis and Treatment	It is highly expressed on the surface of tumors such as neuroendocrine tumors and can be used as a molecular target for PET/CT imaging (e.g. ⁶⁸Ga-DOTATATE) and peptide receptor radionuclide therapy.
Anti-inflammation and Immune Regulation	It is expressed in immune cells, reduces the release of pro-inflammatory factors by inhibiting the NF-κB pathway, and regulates the differentiation and function of T cells.
Metabolic Homeostasis maintenance	It is involved in regulating glucose metabolism, lipid breakdown and gastrointestinal motility. Abnormal functions of it are related to diseases such as metabolic syndrome and diabetes.

The signal transduction of SSTR2 has a typical rapid desensitization characteristic: within minutes after agonist binding, it can trigger receptor internalization through GRK phosphorylation and β-arrestin recruitment. This mechanism not only ensures the fine regulation of the signal but also affects the sustained effect of targeted drugs. Compared with other somatostatin receptor subtypes (such as SSTR5), SSTR2 has a higher affinity for somatostatin -14 and -28, and is the most widely and stably expressed in various tumors, making it the most commonly used subtype in clinical diagnosis and treatment.

Applications of SSTR2 and SSTR2 Antibody in Literature

1. Bo, Qing, et al. "Structural insights into the activation of somatostatin receptor 2 by cyclic SST analogues." Cell Discovery 8.1 (2022): 47. https://doi.org/10.1038/s41421-022-00405-2

This paper analyzed the cryo-electron microscopy structures of the human SSTR2-GI complex that bind SST14, octreotide and lanretide respectively, revealing the key binding sites and selectivity mechanisms of these short-loop peptides in activating SSTR2, providing a structural basis for the development of analogues targeting SSTR2.

2. Zhang, Xiao, et al. "SSTR2 Mediates the Inhibitory Effect of SST/CST on Lipolysis in Chicken Adipose Tissue." Animals 14.7 (2024): 1034. https://doi.org/10.3390/ani14071034

In this study, it was found that highly expressed SSTR2 mediates the anti-fat breakdown effect of somatostatin in chicken adipose tissue. Meanwhile, SSTR2 may promote the proliferation of precursor adipocytes through the MAPK/ERK pathway, thereby regulating adipose tissue development.

3. Gervasoni, Silvia, et al. "Molecular simulations of SSTR2 dynamics and interaction with ligands." Scientific Reports 13.1 (2023): 4768. https://doi.org/10.1038/s41598-023-31823-1

This study analyzed the conformational changes of SSTR2 in the binding agonist, antagonist and ligand-free states through molecular dynamics simulation, revealing the specific interaction mode of ligands on the outer edge of the receptor binding pocket, providing a structural basis for the design of novel targeted drugs.

4. Pivonello, Claudia, et al. "miR-375 regulation of SSTR2 expression in corticotroph pituitary cells: somatostatin receptor ligands effects." Endocrinology 166.8 (2025): bqaf107. https://doi.org/10.1210/endocr/bqaf107

This study reveals that glucocorticoids inhibit the expression of SSTR2 by up-regulating miR-375, reducing the sensitivity of Cushing's patients to octreotide treatment. Inhibition of miR-375 can restore the membrane protein level of SSTR2 and enhance the apoptotic effect induced by octreotide.

5. Ullrich, Martin, et al. "The heterobivalent (SSTR2/albumin) radioligand [67Cu] Cu-NODAGA-cLAB4-TATE enables efficient somatostatin receptor radionuclide theranostics." Theranostics 14.14 (2024): 5371. https://doi.org/10.7150/thno.100091

In this study, a novel copper-67-labeled NODAGA-TATE variant integrating the albumin-binding domain cLAB4 was evaluated in SSTR2-positive tumor models. The results showed that [⁶⁷Cu] Cu-nodaga-CLab4-Tate achieved therapeutic effects comparable to those of the clinical standard drug [¹⁷⁷Lu] LU-dota-Tate by enhancing tumor uptake and prolonging residence time.

Creative Biolabs: SSTR2 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SSTR2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom SSTR2 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our SSTR2 antibodies, custom preparations, or technical support, contact us at email.

Reference

Bo, Qing, et al. "Structural insights into the activation of somatostatin receptor 2 by cyclic SST analogues." Cell Discovery 8.1 (2022): 47. https://doi.org/10.1038/s41421-022-00405-2