Recombinant Mouse DDR1 Fc Chimera Protein, CF

Recombinant Mouse DDR1 Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: DDR1

DDR1, also known as CAK, NEP, CD167a, and EDDR1, is a 120 - 140 kDa type I transmembrane glycoprotein belonging to the discoidin-like domain‑containing subfamily of receptor tyrosine kinases (1, 2). Mature mouse DDR1 consists of a 395 aa extracellular domain (ECD) that includes the discoidin-like domain, a 27 aa transmembrane segment, and a 470 aa cytoplasmic domain with the tyrosine kinase domain (3). Within the ECD, mouse DDR1 shares 93% aa sequence identity with human and rat DDR1, respectively. Alternate splicing of mouse DDR1 generates an additional isoform that lacks a portion of the cytoplasmic domain encompassing the Shc-interacting NPxY motif (4). DDR1 is expressed on epithelial tissues, activated monocytes and neutrophils, smooth muscle cells, and in several cancers (1, 2). It mediates cellular adhesion and migration through interaction of the discoidin-like domain with the triple helical structure of collagens I ‑ V (5, 6). Collagen binding induces prolonged tyrosine autophosphorylation of DDR1, including within the NPxY motif (5, 6). Collagen binding can also induce the metalloproteinase-dependent cleavage of DDR1, thereby liberating a tyrosine phosphorylated 60 kDa C-terminal fragment and a 60 kDa ECD fragment (7, 8). DDR1 is expressed as a dimer on the cell surface independently of ligand binding (9). Oligomerization enhances collagen binding and also modulates collagen fibrillogenesis (10, 11). Collagen-induced activation of DDR1 is inhibited by the association of DDR1 with E-Cadherin at epithelial cell junctions (12). Expression of DDR1 on arterial smooth muscle cells limits smooth muscle cell migration and the development of proteoglycan plaques during atherogenesis (13). The overexpression of particular DDR1 isoforms in glioblastoma promotes MMP-2 activation and increased tumor cell invasiveness (14).

Related Research Areas

• Epithelial Cell Markers and Intracellular Molecules
• Receptor Tyrosine Kinases (RTKs)
• Receptor Tyrosine Kinases (RTKs) in the Akt Pathway
• Surface Ectodermal Cells