Cadherin-1/CD324 Protein, Cynomolgus (HEK293, His)

Cadherin-1/CD324 Protein, a calcium-dependent receptor on myeloid cells, binds to carbohydrates on neutrophils and monocytes. It facilitates interaction between activated endothelial cells or platelets with leukocytes. It recognizes sialyl-Lewis X as its ligand. Through interaction with SELPLG, it mediates rapid leukocyte rolling in early inflammation. Cadherin-1/CD324 Protein also interacts with SNX17 and facilitates neutrophil adhesion and rolling, depending on sialyl-Lewis X epitope and tyrosine sulfation. Cadherin-1/CD324 Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived Cadherin-1/CD324 protein, expressed by HEK293 , with C-His labeled tag. The total length of Cadherin-1/CD324 Protein, Cynomolgus (HEK293, His) is 554 a.a., with molecular weight of 68-78 kDa.

P-Selectin is a calcium-dependent receptor found on myeloid cells that binds to carbohydrates present on neutrophils and monocytes. It plays a crucial role in facilitating the interaction between activated endothelial cells or platelets with leukocytes. The specific ligand recognized by P-Selectin is sialyl-Lewis X. Through its interaction with SELPLG, P-Selectin mediates the rapid rolling of leukocytes over vascular surfaces during the initial stages of inflammation. P-Selectin also interacts with SNX17 and facilitates neutrophil adhesion and leukocyte rolling. This interaction is dependent on the sialyl-Lewis X epitope of SELPLG and PODXL2, as well as specific tyrosine sulfation on SELPLG.

Cynomolgus

HEK293

C-His

A0A2K5V299 (D155-P708)

102143513  [NCBI]

68-78 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.