Enzymes
Product List
DDR1 Human
Discoidin Domain Receptor Tyrosine Kinase 1 Human Recombinant
DDR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 636 amino acids (21-417a.a.) and having a molecular mass of 71.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
DDR1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
DDR2 Human
Discoidin Domain Receptor Tyrosine Kinase 2 Human Recombinant
DDR2 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Introduction
Discoidin Domain Receptor Tyrosine Kinases (DDRs) are a unique class of receptor tyrosine kinases (RTKs) that are activated by collagen. They are distinct from other RTKs due to their ability to bind to and be activated by extracellular matrix proteins rather than peptide growth factors . DDRs are classified into two types: DDR1 and DDR2. DDR1 is primarily expressed in epithelial cells, while DDR2 is found in mesenchymal cells .
Key Biological Properties: DDRs are involved in various fundamental biological processes, including cell adhesion, migration, proliferation, and extracellular remodeling . They exhibit slow and sustained activation kinetics upon collagen binding .
Expression Patterns and Tissue Distribution: DDR1 is predominantly expressed in epithelial cells, including those in the kidney, lung, and brain. DDR2 is mainly found in mesenchymal cells, such as fibroblasts and smooth muscle cells . Both DDR1 and DDR2 are crucial for wound healing and tissue homeostasis .
Primary Biological Functions: DDRs play a significant role in regulating cell-matrix interactions, which are essential for tissue morphogenesis, cell differentiation, and maintenance of tissue architecture . They are also involved in immune responses by mediating immune cell chemotaxis and migration towards infection sites .
Role in Immune Responses and Pathogen Recognition: DDRs contribute to the immune response by facilitating the migration of immune cells to sites of infection and inflammation .
Mechanisms with Other Molecules and Cells: DDRs interact with collagen in the extracellular matrix, leading to their activation. This interaction triggers a cascade of downstream signaling pathways, including MAPK, integrin, TGF-β, insulin receptor, and Notch signaling pathways .
Binding Partners and Downstream Signaling Cascades: Upon activation, DDRs undergo tyrosine phosphorylation, which facilitates the recruitment of various signaling adaptors and effectors. This leads to the activation of multiple downstream signaling pathways that regulate cell proliferation, migration, and survival .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of DDRs are tightly regulated at both transcriptional and post-translational levels. Transcriptional regulation involves various transcription factors that modulate DDR gene expression in response to different stimuli .
Transcriptional Regulation and Post-Translational Modifications: Post-translational modifications, such as phosphorylation, ubiquitination, and glycosylation, play crucial roles in modulating DDR activity and stability .
Biomedical Research: DDRs are valuable targets in biomedical research due to their involvement in various diseases, including cancer, fibrosis, and chronic inflammatory conditions .
Diagnostic Tools and Therapeutic Strategies: DDRs have potential applications in developing diagnostic tools and therapeutic strategies. Inhibitors targeting DDRs are being explored as potential treatments for cancer and other diseases characterized by abnormal DDR activity .
Role Throughout the Life Cycle: DDRs are essential throughout the life cycle, from development to aging. During embryonic development, DDRs regulate tissue morphogenesis and organogenesis . In adulthood, they maintain tissue homeostasis and facilitate wound healing. Dysregulation of DDR activity is associated with various age-related diseases, including cancer and fibrosis .
