Recombinant Human DDR2 Protein, CF

R&D Systems | Catalog # 2538-DR

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Key Product Details

  • R&D Systems NS0-derived Recombinant Human DDR2 Protein (2538-DR)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

Q16832

Applications

Binding Activity
View all DDR2 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human DDR2 protein
Gln24-Arg399, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

No results obtained: Gln24 predicted

Predicted Molecular Mass

43.3 kDa

SDS-PAGE

64-65 kDa, reducing conditions

Activity

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.

Formulation, Preparation, and Storage

2538-DR
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution

Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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. 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).

References

  1. Vogel, W.F. et al. (2006) Cell. Signal. 18:1108.
  2. Karn, T. et al. (1993) Oncogene 8:3433.
  3. Vogel, W. et al. (1997) Mol. Cell 1:13.
  4. Leitinger, B. (2003) J. Biol. Chem. 278:16761.
  5. Leitinger, B. and Kwan, A.P.L. (2006) Matrix Biol. 25:355.
  6. Leitinger, B. et al. (2004) J. Mol. Biol. 344:993.
  7. Mihai, C. et al. (2006) J. Mol. Biol. 361:864.
  8. Olaso, E. et al. (2001) J. Clin. Invest. 108:1369.
  9. Ikeda, K. et al. (2002) J. Biol. Chem. 277:19206.
  10. Xu, L. et al. (2005) J. Biol. Chem. 280:548.
  11. Zhang, Y. et al. (2011) J. Bone Miner. Res. 26:604.
  12. Matsumura, H. et al. (2009) Physiol. Genomics 39:120.
  13. Kano, K. et al. (2010) Mol. Reprod. Dev. 77:29.
  14. Wang, J. et al. (2002) J. Autoimmun. 19:161.
  15. Ferri, N. et al. (2004) Am. J. Pathol. 164:1575.

    Long Name

    Discoidin Domain Receptor 2

    Alternate Names

    TKT, Trk3, Tyro-10

    Entrez Gene IDs

    4921 (Human); 18214 (Mouse)

    Gene Symbol

    DDR2

    UniProt

    Q16832

    Additional DDR2 Products

    Product Documents for Recombinant Human DDR2 Protein, CF

    Certificate of Analysis

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    Note: Certificate of Analysis not available for kit components.

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    Product Specific Notices for Recombinant Human DDR2 Protein, CF

    For research use only

    Related Research Areas

    Receptor Tyrosine Kinases (RTKs)

    Citations for Recombinant Human DDR2 Protein, CF

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    Associated Pathways

    Articular Cartilage Extracellular Matrix Articular Cartilage Extracellular Matrix Thumbnail