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SELPLG

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For Research Use Only. Not For Clinical Use.


Background

The antibody can induce apoptosis upon binding to P-Selectin Glycoprotein Ligand-1 (SELPLG) on activated T cells.
Protein class

Candidate cardiovascular disease genes, CD markers, Plasma proteins

Predicted location

Membrane

Single cell type specificity

Cell type enhanced (dendritic cells, NK-cells, monocytes, Kupffer cells, T-cells, Plasma cells, Macrophages)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Cell line enhanced (HDLM-2, HMC-1, JURKAT, Karpas-707, RPMI-8226, U-266/70, U-266/84)

Interaction

Homodimer; disulfide-linked. Interaction with P-, E- and L-selectins, through their lectin/EGF domains, is required for promoting recruitment and rolling of leukocytes. These interactions require sialyl Lewis X glycan modification but there is a differing dependence for tyrosine sulfations. Sulfation on Tyr-51 of PSGL1 is most important for high affinity L-selectin/SELL binding while P-selectin/SELP requires sulfation on Tyr-48. E-selectin/SELE binds with much lower affinity and requires the sLe(x) epitope, but apparently not tyrosine sulfation. Dimerization appears not to be required for P-selectin/SELP binding. Interacts with SNX20. Interacts with MSN and SYK; mediates the activation of SYK by SELPLG. Interacts with HAVCR1 (PubMed:24703780). (Microbial infection) Interacts with enterovirus 71 capsid proteins. (Microbial infection) Interacts with Staphylococcus aureus proteins SSL5 and SSL11; these interactions prevent SELPLG-mediated neutrophil rolling.

Molecular function

Host cell receptor for virus entry, Receptor

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