Human DDR2 Biotinylated Antibody Summary
Gln24-Arg399
Accession # Q16832
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: 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 (1). 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 (2). 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 (3-5). Collagens II and V are less efficacious ligands (3). DDR2 selectively recognizes the triple helical structure of collagen compared to monomeric or denatured collagen (3, 5, 6). Within collagen II, the D2 period is required for DDR2 binding, and the D1 period is additionally required to trigger DDR2 autophosphorylation (6). The ECD of DDR2 exists as a non-covalent dimer in solution, and dimerization of the receptor greatly enhances collagen binding (4, 7). DDR2 interaction with collagen I inhibits collagen fibrillogenesis and alters collagen fiber morphology (7). Ligand binding induces DDR2 autophosphorylation in the cytoplasmic domain (3, 5, 8), which promotes associations with Shc and Src (9). 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 autophosphorylation (5). Activation of DDR2 by collagen induces upregulation of MMP-1, -2, and -13 as well as DDR2 itself (3, 8, 10). DDR2 is implicated in collagenous matrix destruction and cell invasiveness (8, 10). DDR2 is also upregulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell hyperplasia (8, 10-12).
- Vogel, W.F. et al. (2006) Cell. Signal. 18:1108.
- Karn, T. et al. (1993) Oncogene 8:3433.
- Vogel, W. et al. (1997) Mol. Cell 1:13.
- Leitinger, B. (2003) J. Biol. Chem. 278:16761.
- Leitinger, B. and A.P.L Kwan (2006) Matrix Biol. 25:355.
- Leitinger, B. et al. (2004) J. Mol. Biol. 344:993.
- Mihai, C. et al. (2006) J. Mol. Biol. 361:864.
- Olaso, E. et al. (2001) J. Clin. Invest. 108:1369.
- Ikeda, K. et al. (2002) J. Biol. Chem. 277:19206.
- Xu, L. et al. (2005) J. Biol. Chem. 280:548.
- Wang, J. et al. (2002) J. Autoimmun. 19:161.
- Ferri, N. et al. (2004) Am. J. Pathol. 164:1575.
Product Datasheets
FAQs
No product specific FAQs exist for this product, however you may
View all Antibody FAQsReviews for Human DDR2 Biotinylated Antibody
There are currently no reviews for this product. Be the first to review Human DDR2 Biotinylated Antibody and earn rewards!
Have you used Human DDR2 Biotinylated Antibody?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image
