Human E-Selectin / CD62E Protein, His Tag

Source : 

Human E-Selectin, His Tag (CDE-H5222) is expressed from human 293 cells (HEK293). It contains AA Trp 22 - Pro 556 (Accession # NP_000441.2).

 

Molecule : E-Selectin

 

Synonyms : SELE,RP1-117P20.2,CD62E,ELAM1,ESEL,LECAM2,E-Selectin

 

Format : Powder

 

Category : Bio-Markers & CD Antigens

 

Accession : NP_000441.2

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 59.5 kDa

 

Characteristics :

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 59.5 kDa. The protein migrates as 110 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : PBS, pH7.4

 

Description :

E-Selectin is also known as CD62 antigen-like family member E (CD62E), endothelial-leukocyte adhesion molecule 1 (ELAM-1), or leukocyte-endothelial cell adhesion molecule 2 (LECAM2), a member of the Selectin family, is a 107-115 kDa cell surface glycoprotein. It is transiently expressed on vascular endothelial cells in response to IL-1β and TNFα. E selectin has a cassette structure: an N-terminal, C-type lectin domain, an EGF (epidermal-growth-factor)-like domain, 6 Sushi domain (SCR repeat) units, a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto). During inflammation, E-selectin plays an important part in recruiting leukocytes to the site of injury. The local release of cytokines IL-1 and TNF-α by damaged cells induces the over-expression of E-selectin on endothelial cells of nearby blood vessels. E-selectin mediates the adhesion of tumor cells to endothelial cells, by binding to E-selectin ligands expressed by neutrophils, monocytes, eosinophils, memory-effector T-like lymphocytes, natural killer cells or cancer cells. Furthermore, a number of studies have reported that levels of E-Selectin may be elevated in subjects with a variety of pathological conditions.

 

References :

(1) Collins T, et al., 1991, J. Biol. Chem. 266 (4): 2466–73.
(2) Graves BJ, et al., 1994, Nature 367 (6463): 532–8.
(3) Robbins SL, et al., 1999, Philadelphia: WB Saunders. ISBN 0-7216-7335-X.