Human Recombinant DDR2 protein, hFc Tag (V2LY-0526-LY3529)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
hFc Tag
Protein Construction
This product is Human Recombinant DDR2 protein, hFc Tag consist of Amino Acid: 1-399 and predicts a molecular mass of 69.4 kDa.
Molecule Mass
69.4 kDa
Sequence
Amino Acid: 1-399
Species
Human

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

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Discoidin Domain Receptor Tyrosine Kinase 2
Function
Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416).

It functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.
Biological Process
Biomineral tissue development Source: UniProtKB
Cell adhesion Source: ProtInc
Chondrocyte proliferation Source: UniProtKB
Collagen-activated tyrosine kinase receptor signaling pathway Source: UniProtKB
Collagen fibril organization Source: UniProtKB
Endochondral bone growth Source: UniProtKB
Extracellular matrix organization Source: Reactome
Multicellular organism development Source: GO_Central
Ossification Source: UniProtKB-KW
Peptidyl-tyrosine phosphorylation Source: UniProtKB
Positive regulation of DNA-binding transcription factor activity Source: UniProtKB
Positive regulation of extracellular matrix disassembly Source: UniProtKB
Positive regulation of fibroblast migration Source: UniProtKB
Positive regulation of fibroblast proliferation Source: UniProtKB
Positive regulation of kinase activity Source: GO_Central
Positive regulation of osteoblast differentiation Source: UniProtKB
Positive regulation of protein kinase activity Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Regulation of bone mineralization Source: UniProtKB
Regulation of extracellular matrix disassembly Source: UniProtKB
Regulation of tissue remodeling Source: UniProtKB
Signal transduction Source: ProtInc
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Cellular Location
Cell membrane
Involvement in disease
Spondyloepimetaphyseal dysplasia, short limb-hand type (SEMD-SL):
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.
Warburg-Cinotti syndrome (WRCN):
An autosomal dominant disease characterized by progressive corneal neovascularization, keloid formation, chronic skin ulcers, wasting of subcutaneous tissue, flexion contractures of the fingers, and acro-osteolysis.
Topology
Extracellular: 22-399
Helical: 400-421
Cytoplasmic: 422-855
PTM
N-glycosylated.
Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.

Berestjuk, I., Lecacheur, M., Carminati, A., Diazzi, S., Rovera, C., Prod’homme, V., ... & Tartare‐Deckert, S. (2022). Targeting Discoidin Domain Receptors DDR1 and DDR2 overcomes matrix‐mediated tumor cell adaptation and tolerance to BRAF‐targeted therapy in melanoma. EMBO molecular medicine, 14(2), e11814.

Lin, C. C., Yang, W. H., Lin, Y. T., Tang, X., Chen, P. H., Ding, C. K. C., ... & Chi, J. T. (2021). DDR2 upregulation confers ferroptosis susceptibility of recurrent breast tumors through the Hippo pathway. Oncogene, 40(11), 2018-2034.

Matada, G. S. P., Das, A., Dhiwar, P. S., & Ghara, A. (2021). DDR1 and DDR2: A review on signaling pathway and small molecule inhibitors as an anticancer agent. Medicinal Chemistry Research, 30(3), 535-551.

Barcus, C. E., Hwang, P. Y., Morikis, V., Brenot, A., Pence, P., Clarke, M., & Longmore, G. D. (2021). Tyrosine kinase-independent actions of DDR2 in tumor cells and cancer-associated fibroblasts influence tumor invasion, migration and metastasis. Journal of cell science, 134(19), jcs258431.

Deng, L., Liu, G., Zheng, C., Zhang, L., Kang, Y., & Yang, F. (2019). Circ-LAMP1 promotes T-cell lymphoblastic lymphoma progression via acting as a ceRNA for miR-615-5p to regulate DDR2 expression. Gene, 701, 146-151.

Tu, M. M., Lee, F. Y., Jones, R. T., Kimball, A. K., Saravia, E., Graziano, R. F., ... & Theodorescu, D. (2019). Targeting DDR2 enhances tumor response to anti–PD-1 immunotherapy. Science advances, 5(2), eaav2437.

Bayer, S. V., Grither, W. R., Brenot, A., Hwang, P. Y., Barcus, C. E., Ernst, M., ... & Longmore, G. D. (2019). DDR2 controls breast tumor stiffness and metastasis by regulating integrin mediated mechanotransduction in CAFs. Elife, 8, e45508.

Cario, M. (2018). DDR1 and DDR2 in skin. Cell Adhesion & Migration, 12(4), 386-393.

Grither, W. R., & Longmore, G. D. (2018). Inhibition of tumor–microenvironment interaction and tumor invasion by small-molecule allosteric inhibitor of DDR2 extracellular domain. Proceedings of the National Academy of Sciences, 115(33), E7786-E7794.

Gonzalez, M. E., Martin, E. E., Anwar, T., Arellano-Garcia, C., Medhora, N., Lama, A., ... & Kleer, C. G. (2017). Mesenchymal stem cell-induced DDR2 mediates stromal-breast cancer interactions and metastasis growth. Cell reports, 18(5), 1215-1228.

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

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