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Recombinant Human DDR2 Protein, CF 50 UG

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Recombinant Human DDR2 Protein, CF 50 UG信息二維碼

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產(chǎn)品介紹

    基本參數(shù)

    詳細(xì)說明

    • 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.  

    • 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 K    D <10 nM.    
      Optimal dilutions should be determined by each laboratory for each application.  

    • Source

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

    • Accession #

    • N-terminal Sequence    
      Analysis

      No results obtained: Gln24 predicted

    • Predicted Molecular Mass

      43.3 kDa

    • SDS-PAGE

      64-65 kDa, reducing conditions

    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.


    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.

      1. Long Name:

        Discoidin Domain Receptor 2

      2. Entrez Gene IDs:

        4921 (Human); 18214 (Mouse)

      3. Alternate Names:

        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



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