* Provided that the recommended microplates, buffers, diluents, substrates and solutions
are used, and the assay is run as summarized in the Assay Procedure provided.
This DuoSet IC ELISA contains the basic components required for the development of sandwich ELISAs to measure total DDR1 in cell lysates. An immobilized capture antibody specific for DDR1 binds both phosphorylated and unphosphorylated DDR1. After washing away unbound material, a biotinylated detection antibody is used to detect both phosphorylated and unphosphorylated protein, utilizing a standard Streptavidin-HRP format.
Optimized capture and detection antibody pairings with 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
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
Microplates: From Costar EIA Plate (Costar Catalog # 2592) or 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
Preparation and Storage
Stability & Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
DDR1, also known as CAK, CD167a, RTK6, and TrkE, is a 120-140
kDa type I transmembrane glycoprotein that belongs to the discoidin-like domain containing subfamily of receptor tyrosine kinases and serve as receptors for collagen. DDR1 is expressed on epithelial tissues, activated monocytes and neutrophils, and in several cancers. Compared to isoform DDR1b, DDR1a lacks 37 aa’s that include a Shc-interacting NPxY motif in the cytoplasmic juxtamembrane region.
Two additional kinase deficient splice forms are expressed in colon cancer. The discoidin-like domain mediates binding to collagens I-V.
DDR1 selectively recognizes the triple helical structure of collagen. It is expressed on the cell surface as a dimer which can include different isoforms. DDR1 oligomerization enhances collagen binding and also modulates collagen fibrillogenesis. The transmembrane segment contains a leucine zipper and GxxxG motif, but neither is exclusively required for dimerization. Collagen binding induces prolonged autophosphorylation, including the NPxY motif. Collagen binding also results in the proteolytic cleavage of a tyrosine phosphorylated 60 kDa C-terminal fragment (CTF), and a 60 kDa ECD fragment. TIMP-3 and TAPI-1 inhibit shedding of the ECD fragment but not the CTF. Overexpression of DDR1a promotes MMP-2 activation and results in an increased invasiveness of a glioblastoma cell line; DDR1b does not.
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