E-selectin Human Recombinant
L-selectin Human Recombinant
L-Selectin Human Recombinant, Sf9
Recombinant L-Selectin, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. This protein encompasses amino acids 52-345, corresponding to the extracellular domain, with a molecular weight of approximately 34.1 kDa. Due to glycosylation, it appears as a band around 40-57 kDa on SDS-PAGE. The recombinant protein includes a 6-amino acid Histidine tag at the C-terminus to facilitate purification by affinity chromatography.
Sf9, Baculovirus cells.
P-selectin Human Recombinant
E-Selectin Human Recombinant, HEK
E-Selectin Human Recombinant, Sf9
This recombinant SELE protein is produced in Sf9 insect cells using a baculovirus expression system. It is a single polypeptide chain with a molecular weight of 59.4 kDa. The protein sequence includes amino acids 22 to 556 of the human SELE protein, with a 6-amino acid His-tag added to the C-terminus to facilitate purification. The protein is purified using proprietary chromatographic techniques and is glycosylated, meaning it has sugar molecules attached.
Sf9, Baculovirus cells.
The product is a colorless solution that has been sterilized by filtration.
Selectin P Ligand Human Recombinant
Recombinant Human SELPLG, produced in HEK293 cells, is a single, glycosylated polypeptide chain comprising 496 amino acids (42-295 a.a.). It has a molecular weight of 53.4 kDa. The SELPLG is fused to a 239 amino acid hIgG-His-Tag at its C-terminus and is purified using proprietary chromatographic methods.
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 .
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 .
The expression and activity of selectins are tightly regulated at multiple levels .
Selectins have several applications in biomedical research and clinical practice .