Human DDR1 Biotinylated Antibody Summary
Asp21-Thr416
Accession # Q08345
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: DDR1
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 (1, 2). Mature human DDR2 consists of a 398 amino acid (aa) extracellular domain (ECD) that includes the discoidin-like domain, a 27 aa transmembrane segment, and a 470 aa cytoplasmic region with a tyrosine kinase domain (3). Within the ECD, human DDR1 shares 53% aa sequence identity with human DDR2 and 93% with mouse and rat DDR1. DDR1 is expressed on epithelial tissues, activated monocytes and neutrophils, and in several cancers (2, 4). Compared to isoform DDR1b, DDR1a lacks 37 aa’s that include a Shc-interacting NPxY motif in the cytoplasmic juxtamembrane region (5). Two additional kinase deficient splice forms are expressed in colon cancer (6). The discoidin-like domain mediates binding to collagens I - V (1, 7, 8). DDR1 selectively recognizes the triple helical structure of collagen (7, 8). It is expressed on the cell surface as a dimer which can include different isoforms (5, 9). DDR1 oligomerization enhances collagen binding and also modulates collagen fibrillogenesis (10, 11). The transmembrane segment contains a leucine zipper and GxxxG motif, but neither is exclusively required for dimerization (9). Collagen binding induces prolonged autophosphorylation, including the NPxY motif (7, 8). Collagen binding also results in the proteolytic cleavage of a tyrosine phosphorylated 60 kDa C-terminal fragment (CTF), and a 60 kDa ECD fragment (12, 13). TIMP-3 and TAPI-1 inhibit shedding of the ECD fragment but not the CTF (12). Overexpression of DDR1a promotes MMP-2 activation and results in an increased invasiveness of a glioblastoma cell line; DDR1b does not (14).
- Vogel, W.F. et al. (2006) Cell. Signal. 18:1108.
- Yoshimura, T. et al. (2005) Immunologic Res. 31:219.
- Perez, J.L. et al. (1994) Oncogene 9:211.
- Laval, S. et al. (1994) Cell Growth Differ. 5:1173.
- Perez, J.L. et al. (1996) Oncogene 12:1469.
- Alves, F. et al. (2001) FASEB J. 15:1321.
- Shrivastava, A. et al. (1997) Mol. Cell 1:25.
- Vogel, W. et al. (1997) Mol. Cell 1:13.
- Nordeen, N.A. et al. (2006) J. Biol. Chem. 281:22744.
- Leitinger, B. (2003) J. Biol. Chem. 278:16761.
- Agarwal, G. et al. (2007) J. Mol. Biol. 367:443.
- Slack, B.E. et al. (2006) J. Cell Biochem. 98:672.
- Vogel, W.F. et al. (2001) FEBS Lett. 514:175.
- Ram, R. et al. (2006) J. Neurooncol. 76:239.
Product Datasheets
Citation for Human DDR1 Biotinylated Antibody
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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The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA.
Authors: Huang Y, Arora P, McCulloch CA
J. Cell. Sci., 2009-04-28;122(0):1637-46.
Species: Mouse
Sample Types: Cell Lysates
Applications: Immunoprecipitation, Western Blot
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