L-selectin/CD62L Protein, Mouse (3332a.a, HEK293, His)

L-selectin, a calcium-dependent lectin, binds to glycoproteins on adjacent cells, facilitating lymphocyte attachment to endothelial cells in peripheral lymph nodes. This interaction is essential for leukocyte rolling along the endothelium and requires L-selectin's binding to SELPLG/PSGL1 and PODXL2, dependent on glycan and sulfation modifications. Sulfation of 'Tyr-51' on SELPLG is particularly important for L-selectin binding. L-selectin/CD62L Protein, Mouse (3332a.a, HEK293, His) is the recombinant mouse-derived L-selectin/CD62L protein, expressed by HEK293, with C-His labeled tag. The total length of L-selectin/CD62L Protein, Mouse (3332a.a, HEK293, His) is 332 a.a., with molecular weight of 70-80 kDa.

L-selectin, a calcium-dependent lectin, plays a crucial role in cell adhesion through its binding to glycoproteins on adjacent cells. Specifically, it facilitates the attachment of lymphocytes to endothelial cells in high endothelial venules within peripheral lymph nodes, promoting the initial tethering and rolling of leukocytes along the endothelium. This process requires the interaction of L-selectin with SELPLG/PSGL1 and PODXL2, which is dependent on the sialyl Lewis X glycan modification of SELPLG and PODXL2, as well as the tyrosine sulfation modifications of SELPLG. Notably, the sulfation of 'Tyr-51' on SELPLG is of particular importance for the binding of L-selectin.

Mouse

HEK293

C-His

P18337 (M1-N332)

20343  [NCBI]

70-80 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.