CD62E/E-Selectin Antibody (Mouse mAb) [A9C19]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:500 IF1:40-1:125 FCM1:4000

Application
WB, IP, IHC, IF, FCM, ELISA

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
67 kDa

Positive Control	Human brain (occipital cortex) tissue; HUVEC cells (activated with TNF-a); Human umbilical vein endothelial cells (HUVECs) (rhTNF-a, 25 ng/mL, 6 h)
Negative Control

Datasheet & SDS

Biological Description

Specificity
CD62E/E-Selectin Antibody (Mouse mAb) [A9C19] detects endogenous levels of total CD62E/E-Selectin protein.

Clone
A9C19

Synonym(s)
E-selectin, CD62 antigen-like family member E, Endothelial leukocyte adhesion molecule 1 (ELAM-1), Leukocyte-endothelial cell adhesion molecule 2 (LECAM2), CD62E, SELE, ELAM1

Background
E-selectin, also designated CD62E or ELAM-1, belongs to the selectin family of cell adhesion molecules alongside P-selectin and L-selectin, and is expressed exclusively on vascular endothelial cells following activation by pro-inflammatory cytokines. The extracellular region follows a shared selectin cassette architecture: an N-terminal calcium-dependent C-type lectin domain, followed by an epidermal growth factor-like domain, a series of short consensus repeats, a transmembrane segment, and a cytoplasmic tail, with the lectin domain containing the binding pocket that recognizes glycoconjugates decorated with the tetrasaccharide sialyl Lewis X, the minimal carbohydrate structure required for productive selectin engagement. E-selectin exists in two distinct conformational states distinguished by the interdomain angle formed at the hinge connecting the lectin domain to the EGF-like domain, a bent, low-affinity conformation and an extended, high-affinity conformation, and this hinge region is directly force-responsive: engineered stabilization of the hinge in the extended conformation measurably enhances E-selectin's binding affinity for its ligands specifically under applied mechanical force, directly demonstrating that the hinge angle functions as a force-transducing structural switch governing ligand-binding strength rather than a static architectural feature. Beyond the lectin and EGF domains, the adjacent short consensus repeat domains contribute directly to functional ligand engagement, since E-selectin constructs differing in the number of included short consensus repeats show measurably different glycan-binding profiles and kinetics across a glycan subarray, and dimerization of the extracellular region further modulates binding behavior, establishing that structural elements well beyond the core lectin domain shape which glycan ligands are recognized and how strongly they are bound. Under physiological shear stress conditions, sialyl Lewis X-coated microspheres attach to and roll continuously over E-selectin-coated surfaces within a defined range of wall shear stress, and this rolling behavior depends on E-selectin surface density and shear force, establishing sialyl Lewis X-E-selectin engagement as sufficient on its own, independent of cellular signaling or membrane deformability, to reproduce the characteristic rolling adhesion seen during leukocyte recruitment to inflamed endothelium. This rolling interaction constitutes the initial tethering step of the leukocyte adhesion cascade, slowing circulating neutrophils along the vessel wall before firmer integrin-mediated arrest, and because tumor cells expressing sialyl Lewis X exploit this same E-selectin-dependent rolling and adhesion mechanism on endothelium, E-selectin engagement is additionally implicated in hematogenous cancer metastasis.

Background

E-selectin, also designated CD62E or ELAM-1, belongs to the selectin family of cell adhesion molecules alongside P-selectin and L-selectin, and is expressed exclusively on vascular endothelial cells following activation by pro-inflammatory cytokines. The extracellular region follows a shared selectin cassette architecture: an N-terminal calcium-dependent C-type lectin domain, followed by an epidermal growth factor-like domain, a series of short consensus repeats, a transmembrane segment, and a cytoplasmic tail, with the lectin domain containing the binding pocket that recognizes glycoconjugates decorated with the tetrasaccharide sialyl Lewis X, the minimal carbohydrate structure required for productive selectin engagement. E-selectin exists in two distinct conformational states distinguished by the interdomain angle formed at the hinge connecting the lectin domain to the EGF-like domain, a bent, low-affinity conformation and an extended, high-affinity conformation, and this hinge region is directly force-responsive: engineered stabilization of the hinge in the extended conformation measurably enhances E-selectin's binding affinity for its ligands specifically under applied mechanical force, directly demonstrating that the hinge angle functions as a force-transducing structural switch governing ligand-binding strength rather than a static architectural feature. Beyond the lectin and EGF domains, the adjacent short consensus repeat domains contribute directly to functional ligand engagement, since E-selectin constructs differing in the number of included short consensus repeats show measurably different glycan-binding profiles and kinetics across a glycan subarray, and dimerization of the extracellular region further modulates binding behavior, establishing that structural elements well beyond the core lectin domain shape which glycan ligands are recognized and how strongly they are bound. Under physiological shear stress conditions, sialyl Lewis X-coated microspheres attach to and roll continuously over E-selectin-coated surfaces within a defined range of wall shear stress, and this rolling behavior depends on E-selectin surface density and shear force, establishing sialyl Lewis X-E-selectin engagement as sufficient on its own, independent of cellular signaling or membrane deformability, to reproduce the characteristic rolling adhesion seen during leukocyte recruitment to inflamed endothelium. This rolling interaction constitutes the initial tethering step of the leukocyte adhesion cascade, slowing circulating neutrophils along the vessel wall before firmer integrin-mediated arrest, and because tumor cells expressing sialyl Lewis X exploit this same E-selectin-dependent rolling and adhesion mechanism on endothelium, E-selectin engagement is additionally implicated in hematogenous cancer metastasis.

References
https://pubmed.ncbi.nlm.nih.gov/31949047/ https://pubmed.ncbi.nlm.nih.gov/33633813/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%