DDR2 Antibody (290804) [Alexa Fluor® 488] Summary
Mouse myeloma cell line NS0-derived recombinant human DDR2
Accession # Q16832
Detects human DDR2 in direct ELISAs.
Test in a species/application not listed above to receive a full credit towards a future purchase.
- Flow Cytometry 0.25-1 ug/10^6 cells
Flow Cytometry: Please use 0.25-1 ug of conjugated antibody per 10e6 cells.
Packaging, Storage & Formulations
|Protect from light. Do not freeze.
- 12 months from date of receipt, 2 to 8 °C as supplied.
Supplied in a saline solution containing BSA and Sodium Azide.
0.09% Sodium Azide
Please see the vial label for concentration. If unlisted please contact technical services.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for DDR2 Antibody (290804) [Alexa Fluor® 488]
- CD167 antigen-like family member B
- CD167b antigen
- Discoidin domain receptor 2
- discoidin domain receptor family, member 2
- discoidin domain receptor tyrosine kinase 2
- discoidin domain-containing receptor 2
- EC 2.7.10
- EC 18.104.22.168
- hydroxyaryl-protein kinase
- migration-inducing gene 16 protein
- neurotrophic tyrosine kinase receptor related 3
- Neurotrophic tyrosine kinase, receptor-related 3
- NTRKR3cell migration-inducing protein 20
- Receptor protein-tyrosine kinase TKT
- Tyrosine-protein kinase TYRO10
- tyrosylprotein kinase
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.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed
for 1 year from date of receipt.
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