Mouse DDR1 Kinase / MCK10 / CD167 Protein (His Tag)
6030432F18,AI323681,Cak,CD167a,Nep,PTK3A
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Catalog Number | P50829-M08H |
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Organism Species | Mouse |
Host | Human Cells |
Synonyms | 6030432F18,AI323681,Cak,CD167a,Nep,PTK3A |
Molecular Weight | The secreted recombinant mouse DDR1 comprises 406 amino acids and has a calculated molecular mass of 45.4 kDa. As a result of glycosylation, the apparent molecular mass of rm DDR1 is approximately 50 kDa in SDS-PAGE under reducing conditions. |
predicted N | Asp 20 |
SDS-PAGE | |
Purity | > 95 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the extracellular domain of mouse DDR1 (NP_766550.1) (Met 1-Thr 414) was expressed, with a C-terminal polyhistidine tag. |
Bio-activity | |
Research Area | Developmental Biology |Embryogenesis |Germ Layer Formation |Ectoderm Marker |
Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
Background | Discoidin domain receptor family, member 1 (DDR1), also known as or CD167a (cluster of differentiation 167a), and Mammary carcinoma kinase 10 (MCK10), belongs to a subfamily of tyrosine kinase receptors with an extracellular domain homologous to Dictyostellium discoideum protein discoidin 1. Receptor tyrosine kinases play a key role in the communication of cells with their microenvironment. These kinases are involved in the regulation of cell growth, differentiation and metabolism. Expression of DDR1/MCK10/CD167 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. DDR1/MCK10/CD167 plays an important role in regulating attachment to collagen, chemotaxis, proliferation, and MMP production in smooth muscle cells. DDR1 functions in a feedforward loop to increase p53 levels and at least some of its effectors. Inhibition of DDR1 function resulted in strikingly increased apoptosis of wild-type p53-containing cells in response to genotoxic stress through a caspase-dependent pathway. |
Reference |