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SELPLG

Anti-SELPLG Recombinant Antibody Products

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For Research Use Only. Not For Clinical Use.


SELPLG encodes L - selectin, another key member of the selectin family of cell adhesion molecules. L - selectin is constitutively expressed on the surface of most leukocytes, including neutrophils, lymphocytes, and monocytes. Structurally, it has a similar modular architecture to other selectins, with an N - terminal lectin domain, an epidermal growth factor - like domain, and multiple short consensus repeat domains.
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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