This is clone DREG56, a mouse monoclonal antibody of the IgG1 isotype (mouse host) raised against human CD62L (L-selectin), one of the most widely used and well-validated anti-human L-selectin clones. As an in-vivo-ready, low-endotoxin research reagent supplied in bulk (milligram to gram scale, RUO), it is suited to functional studies that require large, consistent lots and minimal endotoxin-driven artefacts. Reactivity is human-restricted, so the antibody is primarily applied in human cell systems: flow cytometric identification of L-selectin-expressing leukocyte subsets, Western blot detection of the glycoprotein, and blocking/functional assays that interrogate leukocyte adhesion and rolling. Because the target is human, the antibody is a natural fit for ex-vivo work on primary human PBMCs and lymphocyte subsets, as well as for use in humanized-mouse or human-cell adoptive-transfer settings. The low-endotoxin, bulk format supports reproducible functional and adhesion assays where cell activation must be tightly controlled and where reagent lot-to-lot consistency matters across long study timelines.
CD62L (L-selectin, SELL; UniProt P14151) is a type I transmembrane C-type lectin adhesion molecule constitutively expressed on most circulating leukocytes, including naive and central-memory T cells, B cells, monocytes, and neutrophils. Through its lectin domain it binds sialylated, fucosylated, sulfated glycan ligands (such as those presented by GlyCAM-1, CD34, and MAdCAM-1) on high endothelial venules, mediating the initial tethering and rolling that precede firm adhesion and lymphocyte homing to secondary lymphoid organs. L-selectin surface density is dynamically regulated: upon leukocyte activation it is rapidly shed by ADAM17 (TACE)-mediated ectodomain cleavage, so its expression marks less-differentiated, lymph-node-homing subsets and its loss marks effector/effector-memory populations. This makes CD62L a key phenotypic marker for distinguishing naive versus memory T-cell states and a functional node in leukocyte trafficking and inflammation.