CCR7 Antibodies

Structure of CCR7

CCR7 is a G protein-coupled receptor with a molecular weight of approximately 42 kDa. Its precise molecular weight varies slightly among different species, mainly due to conserved variations in amino acid sequences.

CCR7 is composed of 378 amino acids and has a typical seventh-transmembrane domain (TM1-TM7). Its N-terminal contains glycosylation modification sites, while the C-terminal is rich in serine/threonine phosphorylation sites. The ligand-binding pocket of this receptor is mainly composed of TM2, TM3 and TM7, among which the second and third extracellular loops (ECL2/3) determine the specific recognition of CCL19/CCL21.

Fig. 1 Receptor modelling reveals more flexibility for the extracellular loops in the CCR7 dimerisation-defective mutants.¹

Key structural properties of CCR7:

• Seven-time transmembrane helical structure
• Conservative DRY motif
• Extracellular disulfide bond network
• C-terminal phosphorylation site cluster

Functions of CCR7

The core function of the CCR7 gene is to regulate the directional migration and homing of immune cells, and it also plays a key role in various pathophysiological processes.

The signal response of CCR7 exhibits typical dose-dependent gradient sensing characteristics, and its ability to activate the downstream Gαi protein pathway is 3 to 5 times stronger than that of conventional chemokine receptors. This highly efficient signal transduction feature makes it a core regulatory element in the immune cell navigation system. The latest research has found that CCR7 can also activate non-classical signals through the β-Arrestin-dependent pathway and play a continuous regulatory role in chronic inflammation.

Applications of CCR7 and CCR7 Antibody in Literature

1. Lee, Colin YC, et al. "Tumour-retained activated CCR7+ dendritic cells are heterogeneous and regulate local anti-tumour cytolytic activity." Nature Communications 15.1 (2024): 682.https://doi.org/10.1038/s41467-024-44787-1

The article indicates that CCR7+ dendritic cells (DCs) in tumors are heterogeneous: some migrate to the draining lymph nodes, and some remain in the tumor. With the extension of the stay time, the antigen presentation and pro-inflammatory functions of the stranded individuals gradually weakened, but co-localized with PD-1+CD8+ T cells. After anti-PD-L1 treatment, its stimulating molecules such as OX40L are upregulated, enhancing the anti-tumor cytotoxicity. The study revealed the regulatory effect of the functional diversity of CCR7+ DCs on the activation of T cells within tumors.

2. Meloun, Audrey, and Beatriz León. "Beyond CCR7: dendritic cell migration in type 2 inflammation." Frontiers in Immunology 16 (2025): 1558228.https://doi.org/10.3389/fimmu.2025.1558228

The article indicates that traditional dendritic cells (cDCs) rely on CCR7 to migrate to the draining lymph nodes (dLN), but in type 2 immune responses (such as parasitic infections), cDCs still migrate efficiently when CCR7 expression is low. Studies have shown that lipid mediators such as eicosanolic acid and sphingolipids can work in synergy with CCR7 to promote the migration of cDCs and the differentiation of Th2, revealing the unique regulatory mechanism of cDCs migration under type 2 inflammation.

3. Rodríguez-Fernández, José Luis, and Olga Criado-García. "The chemokine receptor CCR7 uses distinct signaling modules with biased functionality to regulate dendritic cells." Frontiers in immunology 11 (2020): 528.https://doi.org/10.3389/fimmu.2020.00528

The article indicates that CCR7 regulates the multifunctionality of dendritic cells (DCs) through modular signaling pathways: the PI3K/Akt pathway maintains survival, MAPK mediates chemotaxis, and RhoA regulates cytoskeletal movement and endocytosis. These pathways are independent of each other and functionally biased, revealing that chemokine receptors can modularly coordinate the pleiotropic functions of white blood cells.

4. Brandum, Emma Probst, et al. "Dendritic cells and CCR7 expression: an important factor for autoimmune diseases, chronic inflammation, and cancer." International journal of molecular sciences 22.15 (2021): 8340. https://doi.org/10.3390/ijms22158340

Research has found that CCR7 and its ligands CCL19/CCL21 play a dual role in chronic inflammation (such as multiple sclerosis and rheumatoid arthritis) and cancer by regulating dendritic cell migration. Targeting CCR7 may lead to the development of anti-inflammatory antagonists and pro-immune agonists, providing new strategies for the immunotherapy of inflammatory diseases and cancer.

5. Gerken, Oliver J., Marc Artinger, and Daniel F. Legler. "Shifting CCR7 towards its monomeric form augments CCL19 binding and uptake." Cells 11.9 (2022): 1444.https://doi.org/10.3390/cells11091444

Research has found that the dimerization state of CCR7 regulates its function: although dimerization defective mutants maintain normal G protein activation ability, they significantly enhance the binding and internalization of CCL19. Structural simulation shows that monization makes the extracellular loop of the receptor more flexible, which may increase the accessibility of ligand binding sites and provide a new mechanism for the functional regulation of CCR7.

Creative Biolabs: CCR7 Antibodies for Research

Creative Biolabs specializes in the production of high-quality CCR7 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom CCR7 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 CCR7 antibodies, custom preparations, or technical support, contact us at email.