CD162/PSGL-1 Protein, Mouse (307a.a, HEK293, Fc)

CD162/PSGL-1 protein, an SLe(x)-type proteoglycan, facilitates early inflammation stages by mediating rapid leukocyte rolling through high-affinity interactions with E- and P-selectins. CD162 forms homodimers linked by disulfide bonds, interacting with selectins through lectin/EGF domains. For high-affinity P-selectin binding, sialyl Lewis X glycan modification and tyrosine sulfation, likely on Tyr-54, are required. Dimerization seems dispensable. CD162 also interacts with SNX20, mediating SYK activation, and with MSN and SYK, contributing to downstream signaling events. Its engagement with HAVCR1 reveals diverse cellular interactions. CD162/PSGL-1 Protein, Mouse (307a.a, HEK293, Fc) is the recombinant mouse-derived CD162/PSGL-1 protein, expressed by HEK293, with C-hFc labeled tag. The total length of CD162/PSGL-1 Protein, Mouse (307a.a, HEK293, Fc) is 307 a.a., with molecular weight of ~82 kDa.

CD162, also known as P-selectin glycoprotein ligand-1 (PSGL-1), functions as an SLe(x)-type proteoglycan and plays a crucial role in the early stages of inflammation by mediating rapid leukocyte rolling over vascular surfaces through high-affinity, calcium-dependent interactions with E- and P-selectins. This interaction is pivotal for the initial capture of leukocytes. CD162 forms homodimers linked by disulfide bonds and interacts with P- and E-selectins through their lectin/EGF domains. For high-affinity binding to P-selectin, sialyl Lewis X glycan modification and tyrosine sulfation, likely on Tyr-54, are required. Dimerization appears dispensable for P-selectin binding. Additionally, CD162 interacts with sorting nexin 20 (SNX20) and mediates SYK activation downstream of P-selectin/SELP binding. Furthermore, CD162 interacts with moesin (MSN) and spleen tyrosine kinase (SYK), contributing to downstream signaling events. It also engages with HAVCR1, revealing its involvement in diverse cellular interactions.

Mouse

HEK293

C-hFc

Q62170 (M1-C307)

20345  [NCBI]

Approximately 82 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.