Target: Discoidin Domain Receptor 1 (DDR1), a receptor tyrosine kinase activated by collagens.
Epitope: Phosphorylated tyrosine 796 (Y796) in the activation loop of DDR1, a site essential for kinase activity .
Cross-reactivity: Detects DDR2 phosphorylated at Y740 due to sequence homology, but exhibits >1,000-fold higher affinity for DDR1 .
| Assay | Dilution | Detection |
|---|---|---|
| Western blot | 0.1–1.0 µg/mL | ~120–130 kDa band (phosphorylated DDR2 cross-reactivity noted) |
| Simple Western | 1.0 µg/mL | Quantitative phosphorylation analysis |
Colorectal Cancer (CRC): DDR1 phosphorylation correlates with metastatic potential. Inhibition of DDR1 via shRNA reduces tumor spread in vivo .
Melanoma: BRAF/MEK inhibitors induce collagen remodeling, activating DDR1 and promoting drug resistance. Co-targeting DDR1 enhances therapeutic efficacy .
Acute Lung Injury (ALI): DDR1 inhibition reduces IL-6/TNF-α release in macrophages, suggesting therapeutic potential .
Pulmonary Fibrosis: DDR1 activation via Y796 phosphorylation mediates fibrotic responses .
DDR1 signaling involves SHP-2 recruitment, leading to downstream MAPK and STAT3 activation .
The Y796 site is critical for kinase activity, with mutations (e.g., Y796F) abrogating signaling .
How to resolve cross-reactivity between DDR1 (Y796) and DDR2 (Y740) in multiplex assays?
How to quantify DDR1 autophosphorylation dynamics in collagen-stimulated signaling?
Inconsistent DDR1 (Y796) signals across cell lines: Technical artifact or biological variation?
Investigation workflow:
How to distinguish DDR1 isoforms (e.g., DDR1a vs. DDR1b) using DDR1 (Ab-796)?
Can DDR1 (Ab-796) be used in non-reducing conditions for dimerization studies?