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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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CD162 Antibody / P-Selectin Glycoprotein Ligand 1 Antibody detects CD162, a cell-surface glycoprotein encoded by the SELPLG gene and widely known as PSGL-1. CD162 functions as a high-affinity counter-receptor for selectins and is expressed on myeloid cells, lymphocytes and other hematopoietic cell populations. Through interactions with P-, E- and L-selectin, PSGL-1 participates in cell adhesion and the recruitment of leukocytes from the circulation into tissues during inflammatory and immune responses.
PSGL-1 is a mucin-like transmembrane glycoprotein whose extracellular region is extensively glycosylated. Functional selectin binding depends on specific post-translational modifications, including tyrosine sulfation and formation of sialyl Lewis x-containing O-glycans. These modifications help generate the high-affinity binding site required for efficient interaction with selectins. PSGL-1 can also form homodimers and contains a cytoplasmic region that connects the receptor with intracellular structural and signaling proteins.
P-Selectin Glycoprotein Ligand 1 is particularly important during the early stages of leukocyte recruitment. Binding between PSGL-1 on circulating leukocytes and selectins on activated endothelial cells or platelets promotes leukocyte tethering and rolling under vascular flow. These initial adhesive interactions help position immune cells for subsequent firm adhesion and migration across the vascular endothelium into sites of inflammation. PSGL-1-mediated interactions are therefore studied in neutrophil, monocyte and lymphocyte trafficking as well as broader mechanisms regulating inflammatory cell recruitment.
CD162 also has functions extending beyond its classical role as an adhesion molecule. Selectin engagement can influence intracellular signaling and immune-cell behavior, while PSGL-1 has been investigated in adaptive immunity, infection and regulation of T-cell responses. Expression and functional glycosylation of PSGL-1 can vary according to cell type and activation state, adding another level of regulation to selectin-dependent leukocyte trafficking. These properties make CD162 relevant to studies of inflammation, immune-cell migration and communication between circulating leukocytes and vascular tissues.
Clone PSGL1/8135R is a recombinant rabbit monoclonal antibody generated against full-length recombinant human protein. It has been evaluated by immunohistochemistry in FFPE human tissues, including tonsil, mammary carcinoma, transverse muscle and lung. Recombinant production provides a defined antibody sequence and supports consistent performance across manufacturing lots. NSJ Bioreagents supplies antibodies for immunology, inflammation and cell adhesion research. A CD162 Antibody can be used to investigate PSGL-1 expression, selectin interactions, leukocyte trafficking and mechanisms regulating inflammatory cell recruitment.
For related antibodies targeting CD molecules involved in immune-cell recognition, adhesion and signaling, explore our CD Antibodies page.
Optimal dilution of the CD162 Antibody / P-Selectin Glycoprotein Ligand 1 Antibody should be determined by the researcher.
Recombinant full-length human protein was used as the immunogen for the CD162 antibody.
Aliquot the CD162 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
CD162 antibody, P-Selectin Glycoprotein Ligand 1 antibody, PSGL-1 antibody, SELPLG antibody, PSGL1 antibody
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