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Mouse Anti-DDR1 Recombinant Antibody (10B6E5A11) (CBMAB-D0500-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Discoidin Domain Receptor Tyrosine Kinase 1 (DDR1). The antibody can be used for immunoassay techniques, such as ELISA, WB.
See all DDR1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
10B6E5A11
Antibody Isotype
IgG
Application
ELISA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Discoidin Domain Receptor Tyrosine Kinase 1
Introduction
DDR1 belongs to a subfamily of tyrosine kinase receptors with homology to Dictyostelium discoideum protein discoidin I in their extracellular domain, and that are activated by various types of collagen. Expression of DDR1 is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, it has been shown to be significantly overexpressed in several human tumors.
Entrez Gene ID
UniProt ID
Alternative Names
Discoidin Domain Receptor Tyrosine Kinase 1; CD167 Antigen-Like Family Member A; Protein-Tyrosine Kinase RTK-6; Mammary Carcinoma Kinase 10; Tyrosine-Protein Kinase CAK; Cell Adhesion Kinase; Tyrosine Kinase DDR; EC 2.7.10.1; EDDR1; NTRK4; PTK3A; HGK2; RTK6; TRKE; CAK; NEP; Epithelial Discoidin Domain-Containing Receptor 1;
Function
Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing (By similarity).

Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11.
Biological Process
Axon development Source: Ensembl
Branching involved in mammary gland duct morphogenesis Source: Ensembl
Cell adhesion Source: ProtInc
Collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
Ear development Source: Ensembl
Embryo implantation Source: Ensembl
Extracellular matrix organization Source: Reactome
Lactation Source: UniProtKB-KW
Mammary gland alveolus development Source: Ensembl
Multicellular organism development Source: GO_Central
Negative regulation of cell population proliferation Source: Ensembl
Neuron projection extension Source: Ensembl
Peptidyl-tyrosine autophosphorylation Source: UniProtKB
Positive regulation of kinase activity Source: GO_Central
Protein autophosphorylation Source: UniProtKB
Regulation of cell growth Source: Ensembl
Regulation of cell-matrix adhesion Source: Ensembl
Regulation of extracellular matrix disassembly Source: UniProtKB
Smooth muscle cell-matrix adhesion Source: UniProtKB
Smooth muscle cell migration Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Wound healing, spreading of cells Source: UniProtKB
Cellular Location
Isoform 1&2&4: Cell membrane
Isoform 3: Secreted
Topology
Extracellular: 21-417
Helical: 418-438
Cytoplasmic: 439-913
PTM
Autophosphorylated in response to fibrillar collagen binding.
Glycosylation of Asn-211, but apparently not of Asn-260 or Asn-394, prevents autophosphorylation from occurring in the absence of collagen.

Zhang, X., Hu, Y., Pan, Y., Xiong, Y., Zhang, Y., Han, M., ... & Zhang, B. (2022). DDR1 promotes hepatocellular carcinoma metastasis through recruiting PSD4 to ARF6. Oncogene, 41(12), 1821-1834.

Chen, L. Y., Zhi, Z., Wang, L., Zhao, Y. Y., Deng, M., Liu, Y. H., ... & Li, J. M. (2019). NSD2 circular RNA promotes metastasis of colorectal cancer by targeting miR‐199b‐5p‐mediated DDR1 and JAG1 signalling. The Journal of Pathology, 248(1), 103-115.

Zhavoronkov, A., Ivanenkov, Y. A., Aliper, A., Veselov, M. S., Aladinskiy, V. A., Aladinskaya, A. V., ... & Aspuru-Guzik, A. (2019). Deep learning enables rapid identification of potent DDR1 kinase inhibitors. Nature biotechnology, 37(9), 1038-1040.

Vehlow, A., & Cordes, N. (2019). DDR1 (discoidin domain receptor tyrosine kinase 1) drives glioblastoma therapy resistance by modulating autophagy. Autophagy, 15(8), 1487-1488.

Moll, S., Desmoulière, A., Moeller, M. J., Pache, J. C., Badi, L., Arcadu, F., ... & Prunotto, M. (2019). DDR1 role in fibrosis and its pharmacological targeting. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1866(11), 118474.

Yeh, Y. C., Lin, H. H., & Tang, M. J. (2019). Dichotomy of the function of DDR1 in cells and disease progression. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1866(11), 118473.

Belfiore, A., Malaguarnera, R., Nicolosi, M. L., Lappano, R., Ragusa, M., Morrione, A., & Vella, V. (2018). A novel functional crosstalk between DDR1 and the IGF axis and its relevance for breast cancer. Cell adhesion & migration, 12(4), 305-314.

Richter, H., Satz, A. L., Bedoucha, M., Buettelmann, B., Petersen, A. C., Harmeier, A., ... & Prunotto, M. (2018). DNA-encoded library-derived DDR1 inhibitor prevents fibrosis and renal function loss in a genetic mouse model of Alport syndrome. ACS chemical biology, 14(1), 37-49.

Takai, K., Drain, A. P., Lawson, D. A., Littlepage, L. E., Karpuj, M., Kessenbrock, K., ... & Werb, Z. (2018). Discoidin domain receptor 1 (DDR1) ablation promotes tissue fibrosis and hypoxia to induce aggressive basal-like breast cancers. Genes & development, 32(3-4), 244-257.

Deng, Y., Zhao, F., Hui, L., Li, X., Zhang, D., Lin, W., ... & Ning, Y. (2017). Suppressing miR-199a-3p by promoter methylation contributes to tumor aggressiveness and cisplatin resistance of ovarian cancer through promoting DDR1 expression. Journal of ovarian research, 10(1), 1-11.

Juskaite, V., Corcoran, D. S., & Leitinger, B. (2017). Collagen induces activation of DDR1 through lateral dimer association and phosphorylation between dimers. Elife, 6, e25716.

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For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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