CD155, also known as PVR (poliovirus receptor), is a 70 kDa type I transmembrane glycoprotein in the nectin-related family of adhesion proteins within the immunoglobulin superfamily. CD155 binds other molecules including Vitronectin, Nectin-3, DNAM-1/CD226, CD96, and TIGIT but does not bind homotypically. Mature human CD155 consists of a 323 aa extracellular domain (ECD) with one N-terminal V-type and two C2-type Ig-like domains, a 24 aa transmembrane segment, and a 50 aa cytoplasmic tail. Within the ECD, human CD155 shares 45% aa sequence identity with mouse and rat CD155, and 52% with human Nectin-2. The V-type domain of CD155 mediates all binding, including to polio virus, and alternative splicing within this domain in humans can modulate ligand binding. Human CD155 can also be spliced to generate secreted isoforms. CD155 is up-regulated on endothelial cells by IFN-gamma and is highly expressed on immature thymocytes, lymph node dendritic cells, and tumor cells of epithelial and neuronal origin. It is preferentially expressed on Th17 cells compared to Th2 cells, and its activation promotes the development of Th1 responses. On migrating cells, CD155 is concentrated at the leading edge, where it binds basement membrane Vitronectin, recruits Nectin-3-expressing cells, and cooperates with PDGF and Integrin alpha v beta 3 to promote cell migration. Enhanced CD155 expression in tumor cells contributes to loss of contact inhibition and increased migration but also allows tumor cell recognition and killing by DNAM-1 or CD96 expressing NK cells.

高纯度、高活性、低内毒素、高批间一致性

产品数据

-25 ~ -15℃保存，收到货之后有效期1年。 复溶后， 无菌条件下，-85 ~ -65℃保存，3个月有效期。