Recombinant Human DDR2 Protein

重组人DDR2蛋白 | 重组人盘状结构域受体家族成员2蛋白

CD167 antigen-like family member B | CD167b antigen | DDR2 | Discoidin domain receptor 2 | discoidin domain receptor family, member 2 | discoidin domain receptor tyrosine kinase 2 | discoidin domain-containing receptor 2 | EC 2.7.10 | EC 2.7.10.1 | hydrox

rp188240-10μg

10μg

无动物源

≥95%(SDS-PAGE)

DDR2, also known as TYR010 and TKT, is a widely expressed 130 kDa type I transmembrane glycoprotein belonging to the discoidin-like domain containing subfamily of receptor tyrosine kinases. Mature human DDR2 consists of a 378 amino acid (aa) extracellular domain (ECD) that includes the discoidin-like domain, a 22 aa transmembrane segment, and a 434 aa cytoplasmic domain that includes the kinase domain. Within the ECD, human DDR2 shares 53% aa sequence identity with DDR1. It shares 97% and 96% aa sequence identity with mouse and rat DDR2, respectively. The discoidin-like domain mediates DDR2 interactions with collagens I, III, and X. Collagens II and V are less efficacious ligands. DDR2 selectively recognizes the triple helical structure of collagen compared to monomeric or denatured collagen. Within collagen II, the D2 period is required for DDR2 binding, while the D1 period is additionally required to trigger DDR2 autophosphorylation. The ECD of DDR2 exists as a noncovalent dimer in solution, and dimerization of the receptor greatly enhances collagen binding. DDR2 interaction with collagen I inhibits collagen fibrillogenesis and alters collagen fiber morphology. Ligand binding induces DDR2 autophosphorylation in the cytoplasmic domain, which promotes associations with Shc and Src. In addition to the above mechanism, DDR2 exhibits a distinct interaction with collagen X. A region other than the discoidin-like domain of DDR2 recognizes the non-helical NC1 domain of collagen X, and this interaction does not lead to receptor autophosphorylation. Activation of DDR2 by collagen induces up-regulation of MMP-1, -2, and -13 as well as DDR2 itself. DDR2 is implicated in collagenous matrix destruction and cell invasiveness. It promotes osteoblast and chondrocyte differentiation and supports ovulation and spermatogenesis. DDR2 is up-regulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell overgrowth diseases. Post-translational: N-glycosylated. Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.

重组表达

43.5 kDa

C-His

48.1-64.8 kDa, under reducing conditions; 48.1-64.8 kDa, under non-reducing conditions.

HEK293 Accession #: Q16832 | HEK293

<1.0 EU/μg

人(Human)

1-399 aa

MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRHHHHHH

Yes

Yes