Human Phospho-DDR2 DuoSet IC ELISA Summary
* Provided that the recommended microplates, buffers, diluents, substrates and solutions are used, and the assay is run as summarized in the Assay Procedure provided.
Product Features
- Optimized capture and detection antibody pairings and recommended concentrations save lengthy development time
- Development protocols are provided to guide further assay optimization
- Assay can be customized to your specific needs
- Available in 2, 5, and 15-(96-well) plate pack sizes
- Economical alternative to Western blot
Kit Content
- Capture Antibody
- Conjugated Detection Antibody
- Calibrated Immunoassay Standard or Control
Other Reagents Required
PBS: (Catalog # DY006), or 137 mM NaCl, 2.7 mM KCl, 8.1 mM Na2HPO4, 1.5 mM KH2O4, pH 7.2 - 7.4, 0.2 µm filtered
Wash Buffer: (Catalog # WA126), or equivalent
Lysis Buffer*
IC Diluent*
Blocking Buffer*
Substrate Solution: 1:1 mixture of Color Reagent A (H2O2) and Color Reagent B (Tetramethylbenzidine) (Catalog # DY999)
Stop Solution: 2 N H2SO4 (Catalog # DY994)
Microplates: R&D Systems (Catalog # DY990), or equivalent
Plate Sealers: ELISA Plate Sealers (Catalog # DY992), or equivalent
*For the Lysis Buffer, IC Diluent, and Blocking BUffer recommended for a specific DuoSet ELISA Development Kit, please see the product
Product Datasheets
Preparation and Storage
Background: DDR2
DDR2, also known as TYR010 and TKT, is a widely expressed 130 kDa type I transmembrane glycoprotein belonging to the discoidin-like domain containing subfamily of receptor tyrosine kinases. Mature human DDR2 consists of a 378 amino acid (aa) extracellular domain (ECD) that includes the discoidin like domain, a 22 aa transmembrane segment, and a 434 aa cytoplasmic domain that includes the kinase domain. Within the ECD, human DDR2 shares 53% aa sequence identity with DDR1 and 97% aa sequence identity with mouse DDR2. The discoidin-like domain mediates DDR2 interactions with collagens I, III, and X. Collagens II and V are less efficacious ligands.
DDR2 selectively recognizes the triple helical structure of collagen compared to monomeric or denatured collagen. Within collagen II, the D2 period is required for DDR2 binding, and the D1 period is additionally required to trigger DDR2 auto-phosphorylation. The ECD of DDR2 exists as a noncovalent dimer in solution, and dimerization of the receptor greatly enhances collagen binding. DDR2 interaction with collagen I inhibits collagen fibrillogenesis and alters collagen fiber morphology. Ligand binding induces DDR2 auto-phosphorylation in the cytoplasmic domain, which promotes associations with Shc and Src. In addition to the above mechanism, DDR2 exhibits a distinct interaction with collagen X. A region other than the discoidin-like domain of DDR2 recognizes the non-helical NC1 domain of collagen X, and this interaction does not lead to receptor auto-phosphorylation. Activation of DDR2 by collagen induces upregulation of MMP1, 2, and 13 as well as DDR2 itself. DDR2 is implicated in collagenous matrix destruction and cell invasiveness. DDR2 is also upregulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell hyperplasia.
Citation for Human Phospho-DDR2 DuoSet IC ELISA
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Phosphoproteomics of collagen receptor networks reveals SHP-2 phosphorylation downstream of wild-type DDR2 and its lung cancer mutants.
Authors: Iwai L, Payne L, Luczynski M, Chang F, Xu H, Clinton R, Paul A, Esposito E, Gridley S, Leitinger B, Naegle K, Huang P
Biochem J, 2013-09-15;454(3):501-13.
Species: Human
Sample Types: Cell Culture Supernates
FAQs
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Which phosphorylated sites are recognized by this assay?
This assay utilizes an anti-phosphorylated tyrosine monoclonal detection antibody, and it recognizes all phosphorylated tyrosine residues.
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