L-selectin/CD62L 蛋白, Human (CHO, His)

L-Selectin, also known as CD62L, is a calcium-dependent lectin that plays a crucial role in mediating cell adhesion by binding to glycoproteins on neighboring cells. Functionally, it facilitates the adherence of lymphocytes to endothelial cells within high endothelial venules in peripheral lymph nodes, promoting the initial tethering and rolling of leukocytes in endothelial tissues. L-Selectin's interaction with SELPLG/PSGL1 and PODXL2 is vital for the recruitment and rolling of leukocytes. This interaction is specifically dependent on the sialyl Lewis X glycan modification of SELPLG and PODXL2, along with tyrosine sulfation modifications of SELPLG. Notably, sulfation on 'Tyr-51' of SELPLG emerges as a critical factor for effective L-Selectin binding. The multifaceted functions of L-Selectin underscore its significance in orchestrating cell adhesion processes and immune cell recruitment. L-selectin/CD62L Protein, Human (CHO, His) is the recombinant human-derived L-selectin/CD62L protein, expressed by CHO , with C-His labeled tag. The total length of L-selectin/CD62L Protein, Human (CHO, His) is 294 a.a., with molecular weight of ~35.6 kDa.

L-选择素，也称为 CD62L，是一种钙依赖性凝集素，通过与邻近细胞上的糖蛋白结合，在介导细胞粘附方面发挥着至关重要的作用。从功能上讲，它促进淋巴细胞粘附到外周淋巴结高内皮微静脉内的内皮细胞，促进内皮组织中白细胞的初始束缚和滚动。 L-选择素与 SELPLG/PSGL1 和 PODXL2 的相互作用对于白细胞的招募和滚动至关重要。这种相互作用特别依赖于 SELPLG 和 PODXL2 的唾液酸路易斯 X 聚糖修饰，以及 SELPLG 的酪氨酸硫酸化修饰。值得注意的是，SELPLG 'Tyr-51' 上的硫酸化成为有效 L-选择蛋白结合的关键因素。 L-选择素的多方面功能强调了其在协调细胞粘附过程和免疫细胞招募中的重要性。

Human

CHO

C-His

P14151 (W39-N332)

6402  [NCBI]

Approximately 35.6 kDa

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

<1 EU/μg, determined by LAL method.