E-Selectin

P16581

Selectins are a family of calcium-dependent type 1 transmembrane proteins. Endothelial (E)-selectin is a heavily glycosylated transmembrane protein expressed by activated endothelial cells in microvascular linings. E-selectin, along with P-selectin and L-selectin, initiate recruitment of circulating leukocytes from blood to sites of inflammation in the vascular lining through interaction with specific cell surface associated carbohydrate determinants. E-selectin consists of an N-terminal type 1 lectin domain, an EGF-like domain, 6 sushi (CCP/SCR) domains, a transmembrane sequence, and a short cytoplasmic domain. Recombinant human E-selectin is a 58.6 kDa protein containing 535 amino acid residues, corresponding to the extracellular portion of the full length protein. Due to glycosylation, E-selectin migrates at an apparent molecular weight of approximately 65-85 kDa by SDS-PAGE analysis under reducing conditions.

535

NM_000450.2

WSYNTSTEAM TYDEASAYCQ QRYTHLVAIQ NKEEIEYLNS ILSYSPSYYW IGIRKVNNVW VWVGTQKPLT EEAKNWAPGE PNNRQKDEDC VEIYIKREKD VGMWNDERCS KKKLALCYTA ACTNTSCSGH GECVETINNY TCKCDPGFSG LKCEQIVNCT ALESPEHGSL VCSHPLGNFS YNSSCSISCD RGYLPSSMET MQCMSSGEWS APIPACNVVE CDAVTNPANG FV

Endothelial leukocyte adhesion molecule 1, ELAM1, CD62E, SELE