L-selectin/CD62L Protein, Cynomolgus (HEK293, Fc)

L-selectin/CD62L, a calcium-dependent lectin, aids cell adhesion by binding neighboring glycoproteins. It mediates lymphocyte adherence to endothelial cells in peripheral lymph nodes, enabling leukocyte tethering and rolling. Interaction with SELPLG/PSGL1 and PODXL2 is vital for leukocyte recruitment and rolling, dependent on sialyl Lewis X glycan modification and tyrosine sulfation of SELPLG. Notably, sulfation on 'Tyr-51' of SELPLG is critical for L-selectin binding. L-selectin/CD62L Protein, Cynomolgus (HEK293, Fc) is the recombinant cynomolgus-derived L-selectin/CD62L protein, expressed by HEK293 , with C-hFc labeled tag. The total length of L-selectin/CD62L Protein, Cynomolgus (HEK293, Fc) is 304 a.a., with molecular weight of ~85 & 35 kDa, respectively.

L-selectin, a calcium-dependent lectin, facilitates cell adhesion by binding to glycoproteins on neighboring cells. It plays a significant role in the adherence of lymphocytes to endothelial cells in high endothelial venules of peripheral lymph nodes and promotes the initial tethering and rolling of leukocytes in endothelial tissues. The interaction between L-selectin and SELPLG/PSGL1 and PODXL2 is crucial for the recruitment and rolling of leukocytes, which relies on the sialyl Lewis X glycan modification of SELPLG and PODXL2, as well as the tyrosine sulfation modifications of SELPLG. Notably, sulfation on 'Tyr-51' of SELPLG is particularly important for the binding of L-selectin.

Cynomolgus

HEK293

C-hFc

Q95198 (D29-N332)

701419  [NCBI]

Approximately 85&35 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.