L-Selectin / CD62L Recombinant Rabbit Monoclonal Antibody [PSH19-78] (HA724102)

UNIPROT #

P18337

PROTEIN NAME

L-Selectin / CD62L

SYNONYMS

A.11 antibody;AI528707 antibody;CD62 antigen ligand antibody;CD62 antigen-like family member L antibody;CD62L antibody;gp90-MEL antibody;IgA nephropathy, susceptibility to, included antibody;L Selectin antibody;L-selectin antibody;LAM-1 antibody;LAM1 antibody;LECAM1 antibody;LEU8 antibody;Leukocyte adhesion molecule 1 antibody;Leukocyte surface antigen Leu-8 antibody;Leukocyte-endothelial cell adhesion molecule 1 antibody;Lnhr antibody;LSEL antibody;Ly-22 antibody;Ly-m22 antibody;Lyam-1 antibody;LYAM1 antibody;LYAM1_HUMAN antibody;Lymph node homing receptor antibody;Lymphocyte adhesion molecule 1 antibody;Lymphocyte antigen 22 antibody;Lymphocyte surface MEL-14 antigen antibody;MEL-14 antibody;Pln homing receptor antibody;PLNHR antibody;Selectin L antibody;Selectin, lymphocyte antibody;SELL antibody;TQ1 antibody

SUBCELLULAR LOCATION

Cell membrane.

FUNCTION

L-selectin, also known as CD62L, is a cell adhesion molecule found on the cell surface of leukocytes, and the blastocyst. It is coded for in the human by the SELL gene. L-selectin belongs to the selectin family of proteins, which recognize sialylated carbohydrate groups containing a Sialyl LewisX (sLeX) determinant. L-selectin plays an important role in both the innate and adaptive immune responses by facilitating leukocyte-endothelial cell adhesion events. These tethering interactions are essential for the trafficking of monocytes and neutrophils into inflamed tissue as well as the homing of lymphocytes to secondary lymphoid organs. L-selectin is also expressed by lymphoid primed hematopoietic stem cells and may participate in the migration of these stem cells to the primary lymphoid organs. In addition to its function in the immune response, L-selectin is expressed on embryonic cells and facilitates the attachment of the blastocyst to the endometrial endothelium during human embryo implantation. L-selectin is composed of multiple structural regions: an N-terminus C-type lectin domain, an adjacent epidermal growth factor-like domain, two to the consensus repeat units homologous to those found in C3/C4-binding proteins, an extracellular cleavage site, a short transmembrane domain, and a cytoplasmic tail. It is cleaved by ADAM17.