R-phycoerythrin (PE) is a stable and highly soluble phycobiliprotein which provides maximal absorbance and fluorescence without susceptibility to internal or external fluorescence quenching, thus providing an exceptional quantum yields and molar extinction coefficients.
NCAM, as a member of the immunoglobulin superfamily of adhesion molecules is characterized by several immunoglobulin (Ig)-like domains. The extracellular part of NCAM consists of five of these Ig domains and two fibronectin type III homology regions. NCAM is encoded by a single copy gene composed of 26 exons. However, at least 20-30 distinct isoforms can be generated by alternative splicing and by posttranslational modifications, such as sialylation. During sialylation, polysialic acid (PSA) carbohydrates are attached to the extracellular part of NCAM. Through its extracellular region, NCAM mediates homophilic interactions. In addition, NCAM can also undergo heterophilic interactions by binding extracellular matrix components, such as laminin, or other cell adhesion molecules, such as integrins.
Analyte Specific Reagent
Protein Aliases: antigen recognized by monoclonal antibody 5.1H11; CD56; N-CAM-1; Neural cell adhesion molecule 1; neural cell adhesion molecule, NCAM
Gene Aliases: CD56; MSK39; NCAM; NCAM1
UniProt ID: (Human) P13591
Entrez Gene ID: (Human) 4684
Molecular Function: cell adhesion molecule cytokine receptor defense/immunity protein hydrolase immunoglobulin receptor superfamily immunoglobulin superfamily cell adhesion molecule phosphatase protein phosphatase receptor