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DDR2/CD167b  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: Baculovirus-Insect Cells  
10209-H20B1-50
10209-H20B1-20
50 µg 
20 µg 
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Expression host: Human Cells  
10209-H02H-50
10209-H02H-100
50 µg 
100 µg 
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Expression host: Human Cells  
10209-H08H-50
10209-H08H-100
50 µg 
100 µg 
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Description: Active  
Expression host: Human Cells  
50541-M08H-50
50541-M08H-100
50 µg 
100 µg 
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Expression host: Human Cells  
80341-R02H-50
80341-R02H-100
50 µg 
100 µg 
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Expression host: Human Cells  
80341-R08H-50
80341-R08H-20
50 µg 
20 µg 
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Expression host: Human Cells  
90228-C02H-50
90228-C02H-100
50 µg 
100 µg 
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Expression host: Human Cells  
90228-C08H-50
90228-C08H-100
50 µg 
100 µg 
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DDR2/CD167b Related Area

DDR2/CD167b Related Pathways

    DDR2/CD167b Summary & Protein Information

    DDR2/CD167b Background

    Gene Summary: Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation, and metabolism. In several cases the biochemical mechanism by which RTKs transduce signals across the membrane has been shown to be ligand induced receptor oligomerization and subsequent intracellular phosphorylation. This autophosphorylation leads to phosphorylation of cytosolic targets as well as association with other molecules, which are involved in pleiotropic effects of signal transduction. RTKs have a tripartite structure with extracellular, transmembrane, and cytoplasmic regions. This gene encodes a member of a novel subclass of RTKs and contains a distinct extracellular region encompassing a factor VIII-like domain. Alternative splicing in the 5' UTR results in multiple transcript variants encoding the same protein.
    General information above from NCBI
    Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:20004161}.
    Enzyme regulation: ENZYME REGULATION: Present in an inactive state in the absence of collagen binding and phosphorylation by SRC. Tyrosine phosphorylation enhances the affinity for ATP and the catalytic activity. {ECO:0000269|PubMed:16186108}.
    Subunit structure: Binds hydroxyproline-rich sequence motifs in fibrillar, glycosylated collagen, such as the GQOGVMGFO motif, where O stands for hydroxyproline. Interacts with SRC. Interacts (tyrosine phosphorylated) with SHC1. {ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:17703188, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161}.
    Subcellular location: Cell membrane {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}; Single-pass type I membrane protein {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}.
    Tissue specificity: Detected in osteocytes, osteoblastic cells in subchondral bone, bone lining cells, tibia and cartilage (at protein level). Detected at high levels in heart and lung, and at low levels in brain, placenta, liver, skeletal muscle, pancreas, and kidney. {ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:8247548}.
    Induction: Up-regulated during osteoblast differentiation (in vitro). Up-regulated in cartilage from osteoarthritis patients. {ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:20564243}.
    Post-translational: N-glycosylated. {ECO:0000269|PubMed:20223752}.; Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues. {ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:9659899}.
    Involvement in disease: DISEASE: Spondyloepimetaphyseal dysplasia short limb-hand type (SEMD-SL) [MIM:271665]: A bone disease characterized by short-limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping. {ECO:0000269|PubMed:19110212, ECO:0000269|PubMed:20223752}. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 F5/8 type C domain. {ECO:0000255|PROSITE-ProRule:PRU00081}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.
    General information above from UniProt

    Discoidin domain receptor 2 (DDR2) or CD167b (cluster of differentiation 167b) is a kind of protein tyrosine kinases associated with cell proliferation and tumor metastasis, and collagen, identified as a ligand for DDR2, up-regulates matrix metallloproteinase 1 (MMP-1) and MMP-2 expression in cellular matrix. DDR2/CD167b was found to recognise the triple-helical region of collagen X as well as the NC1 domain. Binding to the collagenous region was dependent on the triple-helical conformation. DDR2/CD167b autophosphorylation was induced by the collagen X triple-helical region but not the NC1 domain, indicating that the triple-helical region of collagen X contains a specific DDR2 binding site that is capable of receptor activation. DDR2/CD167b is induced during stellate cell activation and implicate the phosphorylated receptor as a mediator of MMP-2 release and growth stimulation in response to type I collagen. Moreover, type I collagen-dependent upregulation of DDR2/CD167b expression establishes a positive feedback loop in activated stellate cells, leading to further proliferation and enhanced invasive activity.

    Immune Checkpoint   Immunotherapy   Cancer Immunotherapy   Targeted Therapy

    DDR2/CD167b Alternative Name

    TKT,MIG20a,NTRKR3,TYRO10, [homo-sapiens]
    CD167b,DDR2,MIG20a,NTRKR3,RP11-572K18.1,TKT,TYRO10, [human]
    AW495251,CD167b,Ddr2,Ntrkr3,tyro10, [mouse]
    Ntrkr3,tyro10,AW495251, [mus-musculus]

    DDR2/CD167b Related Studies

  • Olaso E, et al. (2001) DDR2 receptor promotes MMP-2-mediated proliferation and invasion by hepatic stellate cells. J Clin Invest. 108(9): 1369-78.
  • Zhang W, et al. (2006) Expression of discoidin domain receptor 2 (DDR2) extracellular domain in pichia pastoris and functional analysis in synovial fibroblasts and NIT3T3 cells. Mol Cell Biochem. 290(1-2): 43-53.
  • Leitinger B, et al. (2006) The discoidin domain receptor DDR2 is a receptor for type X collagen. Matrix Biol. 25(6): 355-64.
  • Leitinger B, et al. (2004) The D2 period of collagen II contains a specific binding site for the human discoidin domain receptor, DDR2. J Mol Biol. 344(4): 993-1003.
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