Recombinant Proteins
Product List
E Selectin Human
E-selectin Human Recombinant
L Selectin Human
L-selectin Human Recombinant
L-Selectin Human, Sf9
L-Selectin Human Recombinant, Sf9
L-Selectin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 303 amino acids (52-345a.a.) and having a molecular mass of 34.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
L-Selectin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
P Selectin Human
P-selectin Human Recombinant
SELE Human, HEK
E-Selectin Human Recombinant, HEK
SELE Human, Sf9
E-Selectin Human Recombinant, Sf9
SELE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids (22-556 a.a) and having a molecular mass of 59.4kDa.
SELE is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Sterile filtered colorless solution.
SELPLG Human
Selectin P Ligand Human Recombinant
SELPLG Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 496 amino acids (42-295 a.a) and having a molecular mass of 53.4kDa.
SELPLG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Introduction
Selectins are a family of cell adhesion molecules (CAMs) that play a crucial role in mediating the interaction between leukocytes and endothelial cells. They are single-chain transmembrane glycoproteins that share properties with C-type lectins due to their calcium-dependent binding to sugar moieties . There are three main types of selectins:
Selectins are characterized by their ability to bind to specific carbohydrate structures on the surfaces of cells. They have a modular structure consisting of an N-terminal lectin domain, an epidermal growth factor (EGF)-like domain, a series of consensus repeat units, a transmembrane domain, and a cytoplasmic tail .
- Expression Patterns: L-selectin is expressed on most leukocytes, E-selectin is induced on endothelial cells by inflammatory cytokines, and P-selectin is stored in granules of platelets and endothelial cells .
- Tissue Distribution: L-selectin is found on leukocytes, E-selectin on endothelial cells, and P-selectin on platelets and endothelial cells .
Selectins mediate their effects through binding to specific carbohydrate ligands on the surfaces of other cells . This interaction is calcium-dependent and involves the lectin domain of the selectin molecule .
- Binding Partners: The primary ligands for selectins include sialyl Lewisx and P-selectin glycoprotein ligand-1 (PSGL-1) .
- Downstream Signaling Cascades: Binding of selectins to their ligands triggers intracellular signaling pathways that lead to changes in cell behavior, such as increased adhesion and migration .
The expression and activity of selectins are tightly regulated at multiple levels .
- Transcriptional Regulation: Inflammatory cytokines such as TNF-α and IL-1β induce the expression of E-selectin on endothelial cells .
- Post-translational Modifications: Selectins undergo various post-translational modifications, including glycosylation, which are essential for their proper function .
Selectins have several applications in biomedical research and clinical practice .
- Biomedical Research: They are used as markers to study inflammation and immune responses .
- Diagnostic Tools: Selectins can be used as biomarkers for inflammatory diseases and certain cancers .
- Therapeutic Strategies: Targeting selectins and their ligands is being explored as a therapeutic approach for treating inflammatory diseases and preventing cancer metastasis .
