LYVE1 Monoclonal Antibody (ALY7), Alexa Fluor™ 488, eBioscience™, Invitrogen™

Description

Description: The monoclonal antibody ALY7 recognizes mouse LYVE-1, a transmembrane glycoprotein with similarity to CD44. The extracellular domain contains a conserved hyaluro binding domain also found in CD44. Expression is found on lymphatic and liver endothelial cells and some populations of macrophages. The lymphatic system is responsible for transporting proteins and cells (especially dendritic cells) to tissues throughout the body, thereby acting as immune surveyors. LYVE-1 is one characteristic protein, along with podoplanin, PROX-1, Tie-2 and VEGFR-3, that is expressed on lymphatic endothelial cells (LECS). The ligand for LYVE-1 is hyaluro, a large mucopolysaccharide. Although LYVE-1 can bind hyaluro in vitro, the site for ligand binding in vivo is masked by sialyated O-linked glycan chains. It is postulated that binding to ligand requires modification/unmasking to expose the binding site. The development and remodeling of the endothelium after injury is an area of extensive study. When transplanted, hematopoietic stem cells (HSCs) can give rise to LECs that integrate into the endothelium in normal and metastatic tissue. Applications Reported: This ALY7 antibody has been reported for use in flow cytometric analysis and immunohistologic staining of frozen tissue sections. Applications Tested: This ALY7 antibody has been tested by immunofluorescence microscopy on mouse intestine. This can be used at less than or equal to 2 μg/mL.

LYVE1 has been identified as a major receptor for HA (extracellular matrix glycosaminoglycan hyaluronan) on the lymph vessel wall. The deduced amino acid sequence of LYVE1 predicts a 322-residue type I integral membrane polypeptide 41% similar to the CD44 HA receptor with a 212-residue extracellular domain containing a single Link module, the prototypic HA binding domain of the Link protein superfamily. Like CD44, the LYVE1 molecule binds both soluble and immobilized HA. However, unlike CD44, the LYVE1 molecule colocalizes with HA on the luminal face of the lymph vessel wall and is completely absent from blood vessels. Hence, LYVE1 is the first lymph-specific HA receptor to be characterized and is a uniquely powerful marker for lymph vessels themselves. LYVE1 is a type I integral membrane glycoprotein. LYVE-1 is expressed primarily on lymphatic vessel endothelium and is likely to be involved in regulating the traffic of leucocytes and tumor cells to lymph nodes. The lymphatic vasculature forms a second circulatory system that drains extracellular fluid from the tissues and provides an exclusive environment in which immune cells can encounter and respond to foreign antigen. A number of molecules have been identified as markers for lymphatic endothelium which include LYVE1, PALE, VEGFR3, and podoplanin. Diseases associated with LYVE1 dysfunction includes Complete Androgen Insensitivity Syndrome.