Measured by its binding ability in a functional ELISA. Immobilized Collagen I at 10 µg/mL (100 µL/well) can bind Recombinant Human DDR2 with an apparent KD <10 nM. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human DDR2 protein Gln24-Arg399, with a C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
43.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
64-65 kDa, reducing conditions
Publications
Read Publication using 2538-DR in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human DDR2 Protein, CF
CD167 antigen-like family member B
CD167b antigen
DDR2
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 2.7.10.1
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
TKT
TKTMIG20a
Trk3
TYRO10
Tyro-10
Tyrosine-protein kinase TYRO10
tyrosylprotein kinase
Background
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. It shares 97% and 96% aa sequence identity with mouse and rat DDR2, respectively. 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. The D1 period is additionally required to trigger DDR2 autophosphorylation (6). The ECD of DDR2 exists as a noncovalent 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 up‑regulation 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). It promotes osteoblast and chondrocyte differentiation and supports ovulation and spermatogenesis (11-13). DDR2 is up‑regulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell overgrowth diseases (8, 10, 14, 15).
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 Kwan, A.P.L. (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.
Zhang, Y. et al. (2011) J. Bone Miner. Res. 26:604.
Matsumura, H. et al. (2009) Physiol. Genomics 39:120.
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