DDR1 Antibodies

Structure of DDR1

DDR1 is a transmembrane receptor protein with a molecular weight of approximately 120 kDa. Its exact molecular weight varies depending on different splicing variants and the degree of glycosylation modification.

This protein is composed of a polypeptide chain of approximately 910 amino acid residues, and its extracellular region contains a unique disc-shaped domain responsible for specific recognition and binding to collagen. This domain forms a unique β -barrel fold, constituting a key interface for interaction with collagen. The transmembrane region conducts extracellular signals into the intracellular, and its intracellular part contains a typical tyrosine kinase domain that activates downstream signaling pathways through autophosphorylation.

Fig. 1 Schematic diagram of wild-type and signalling-defective DDR1 mutants.¹

Key structural properties of DDR1:

• Extracellular disc-shaped domains mediate collagen recognition and binding
• The single transmembrane helix is responsible for signal transduction
• Intracellular tyrosine kinase domains catalyze self and substrate phosphorylation
• The conserved DFG and HRD motifs in the kinase domain are crucial for regulating enzyme activity

Functions of DDR1

The main function of DDR1 is to act as a cell surface receptor for collagen, mediating signal transduction between cells and the matrix. However, it is also widely involved in a variety of pathophysiological processes, including tissue development, fibrosis and tumor progression.

Unlike the ligands of most receptor tyrosine kinases (mostly soluble growth factors), the ligand of DDR1 is insoluble collagen, which leads to its slow activation but persistent signaling, playing a unique role in the long-term adaptation of cells to the hardness and composition of the tissue microenvironment.

Applications of DDR1 and DDR1 Antibody in Literature

1. Zhang, Xiaochao, et al. "DDR1 promotes hepatocellular carcinoma metastasis through recruiting PSD4 to ARF6." Oncogene 41.12 (2022): 1821-1834. https://doi.org/10.1038/s41388-022-02212-1

The article indicates that in liver cancer, the expression of DDR1 is elevated and associated with a poor prognosis. Research has found that DDR1 activates ARF6 by recruiting PSD4, thereby regulating the ERK/MAPK signaling pathway and promoting the migration, invasion and lung metastasis of liver cancer cells. DDR1 and ARF6 are expected to become new targets for the treatment of liver cancer.

2. Zhang, Jin, et al. "DDR1 promotes metastasis of cervical cancer and downstream phosphorylation signal via binding GRB2." Cell Death & Disease 15.11 (2024): 849. https://doi.org/10.1038/s41419-024-07212-5

The article indicates that in cervical cancer, the oncogene SOX2 positively regulates the expression of DDR1. DDR1 directly binds to GRB2, activates downstream phosphorylation signals, enhances the migration, invasion and epithelial-mesenchymal transition capabilities of cancer cells, and ultimately promotes lung metastasis. DDR1 is a potential therapeutic target for cervical cancer.

3. Su, Hua, et al. "Collagenolysis-dependent DDR1 signalling dictates pancreatic cancer outcome." Nature 610.7931 (2022): 366-372. https://doi.org/10.1038/s41586-022-05169-z

The article indicates that in pancreatic cancer, collagen regulates tumor fate through DDR1: cleaved collagen activates the DDR1-NF-κB-NRF2 pathway, promoting tumor growth and metastasis; Intact collagen induces the degradation of DDR1 and inhibits tumor progression. DDR1 is a potential therapeutic target.

4. Wei, Zhewei, et al. "DDR1 Drives Malignant Progression of Gastric Cancer by Suppressing HIF‐1α Ubiquitination and Degradation." Advanced Science 11.35 (2024): 2308395. https://doi.org/10.1002/advs.202308395

The article indicates that in gastric cancer, DDR1 enhances tumor angiogenesis by directly binding to HIF-1α and inhibiting its ubiquitination. Meanwhile, the DDR1-HIF-1α axis activates the RhoA/ROCK1 signaling, reshapes the cytoskeleton, and thereby promotes gastric cancer metastasis. Targeted inhibition of DDR1 can effectively inhibit tumor progression, indicating that it can be used as a therapeutic target for gastric cancer.

5. Corcoran, David S., et al. "DDR1 autophosphorylation is a result of aggregation into dense clusters." Scientific reports 9.1 (2019): 17104. https://doi.org/10.1038/s41598-019-53176-4

Research has found that collagen activates the kinase function of DDR1 receptors by inducing their aggregation on the membrane. DDR1 first forms unphosphorylated clusters, which then further aggregate and transform into a phosphorylated state. This process depends on its transmembrane region but does not require kinase activity, which explains its slow activation characteristic.

Creative Biolabs: DDR1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality DDR1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom DDR1 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 DDR1 antibodies, custom preparations, or technical support, contact us at email.