Phospho-DDR2 (Y740) and Total DDR2 ELISA Kit is a Semi-quantitative ELISA kit for the measurement of Phospho-DDR2 (Y740) and Total DDR2 in Human in Cell Lysate samples.
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Phospho-DDR2 (Y740) and Total DDR2 ELISA Kit is a Semi-quantitative ELISA kit for the measurement of Phospho-DDR2 (Y740) and Total DDR2 in Human in Cell Lysate samples.
Phospho-DDR2 (Tyr740) and Total DDR2 ELISA Kit (ab279771) is a very rapid, convenient, and sensitive assay kit that can monitor the activation or function of important biological pathways in human cell lysates. By determining phosphorylated DDR2 protein in your experimental model system, you can verify pathway activation in your cell lysates. You can simultaneously measure numerous different cell lysates without spending excess time and effort in performing a Western Blotting analysis.
This Sandwich ELISA kit is an in vitro enzyme-linked immunosorbent assay for the measurement of human phospho-DDR2 (Tyr740) and total DDR2. An anti-pan DDR2 antibody has been coated onto a 96-well plate. Samples are pipetted into the wells and DDR2 present in a sample is bound to the wells by the immobilized antibody and the wells are washed. In select wells, rabbit anti-phospho DDR2 (Tyr740) antibody is added to detect phosphorylated DDR2 (Tyr740). In the remaining wells, rabbit anti-pan-DDR2 antibody is used to detect pan DDR2. After washing away unbound antibody, HRP-conjugated anti-rabbit IgG is pipetted into the wells. The wells are again washed, a TMB substrate solution is added to the wells and color develops in proportion to the amount of DDR2 (Tyr740) or pan DDR2 bound. The Stop Solution changes the color from blue to yellow, and the intensity of the color is measured at 450 nm.
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The Discoidin Domain Receptor 2 (DDR2) also known as Tyrosine-protein kinase DDR2 is a receptor tyrosine kinase that binds to collagen initiating various cellular processes. It has a molecular mass of approximately 97 kDa. This receptor is expressed in various tissues including skin bone and cartilage as well as in certain cancer cells. DDR2 activation is achieved through the recognition of specific motifs such as GFOGER in collagen leading to signaling cascades that impact cell functions like adhesion proliferation and extracellular matrix remodeling.
DDR2 functions as an integral part of the cellular response to collagen. The receptor plays a critical role in the development and maintenance of connective tissues. It exists as a monomer but can form complexes upon ligand binding facilitating its activity. DDR2 signaling influences critical processes such as wound healing and tissue homeostasis by modulating matrix metalloproteinases (MMPs) activity which are important for remodeling the extracellular matrix.
DDR2 abettors collagen-induced signal transduction particularly within the mitogen-activated protein kinase (MAPK) pathway and the Src family kinase pathway. These pathways involve proteins like SHP2 and Src both of which interact with DDR2 to propagate cellular signals. DDR2 activation leads to phosphorylation events that stimulate cytoskeletal rearrangements and gene expression modulations relevant to cellular growth and differentiation.
DDR2 is linked to fibrosis and cancer. The receptor's overexpression or aberrant signaling can contribute to fibrotic diseases characterized by excessive scarring by promoting collagen deposition and fibroblast proliferation. In cancer DDR2 dysregulation often associates with tumor progression and metastasis particularly in lung cancer and sarcomas. This links DDR2 with other oncogenic proteins and pathways including those governed by MMP proteins which are involved in tumor invasion and metastasis.
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Positive Control.
Jurkat cells were treated with PV (Pervanadate).
Solubilize cells at 4 x 107 cells/ml in Cell Lysate Buffer.
Serial dilutions of lysates were analyzed in this ELISA.
Jurkat cells were treated with/without Calyculin A and Pervanadate. Jurkat cells were treated or untreated with Calyculin A and Pervanadate.
Jurkat cells were treated with/without Calyculin A and Pervanadate. Jurkat cells were treated or untreated with Calyculin A and Pervanadate.
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