DDR1 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 Cells. The accession number is NP_001189452.2.

Human

HEK293 Cells

TRKE,RTK6,PTK3A,PTK3,NTRK4,NEP,MCK10,HGK2,EDDR1,DDR,CD167,CAK

A DNA sequence encoding the Human DDR1 (NP_001189452.2) (Met1-Thr416) was expressed with a C-terminal polyhistidine tag followed by an AVI tag. The expressed protein was biotinylated in vivo by the Biotin-Protein ligase (BirA enzyme) which is co-expressed.

≥ 95% as determined by SDS-PAGE. ≥ 95% as determined by SEC-HPLC.

Please refer to the lot-specific COA.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

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.