Reactivity | RtSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of LS180 human colorectal adenocarcinoma cells. When 5 x 104 cells/well are added to Recombinant Rat L‑Selectin/CD62L Fc Chimera coated plates, adhesion is induced in a dose dependent manner after a 1 hour incubation at 37 °C. The ED50 for this effect is 0.4‑2 μg/mL. |
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Source | Mouse myeloma cell line, NS0-derived rat L-Selectin/CD62L protein
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Accession # | |||||||
N-terminal Sequence | Trp39 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Sell |
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Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 60 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE | 90-96 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
L-Selectin (also known as Leukocyte Selectin, LAM-1, LECAM-1, LECCAM-1, TQ1, Leu-8, MEL-14 antigen, DREG, lymph node homing receptor, CD62L) is a member of the Selectin family of cell surface molecules which include E-Selectin and P-Selectin. All Selectins have an extracellular domain composed of an amino-terminal calcium-dependent lectin domain, an epidermal growth factor (EGF)-like domain, two to nine short consensus repeat (SCR) units, a transmembrane domain, and a cytoplasmic tail. L-Selectin expression is limited to hematopoietic cells, with most leukocytes expressing L-Selectin at some stage of differentiation. The majority of myeloid cells, B cells, and virgin T cells express L-Selectin, while only a sub-population of memory T cells and NK cells express L-Selectin. Lymphocytes and neutrophils exhibit a reversible loss of L-Selectin after cellular activation that results from endoproteolytic release of the extracellular portion of receptor from the cell surface. Cleavage of L-Selectin from the cell surface results in a high circulating level of functionally active soluble L-Selectin. All selectins bind sialytated and fucosylated oligosaccharides that are linked to glycoproteins and glycolipids. L-Selectin specifically binds to at least three different heavily glycosolylated mucin-like proteins: GlyCAM-1, CD34, and MAdCAM-1. Multiple studies indicated that L-Selectin, P-Selectin E-Selectin collaborate to mediate the initial binding of leukocytes to endothelium at sites of tissue injury and inflammation, producing the characteristic “rolling” of leukocytes along the endothelium. L-Selectin knockout mice have a 70% decrease in rolling leukocytes in exposed mesentery and have impaired neutrophil and monocyte migration into areas of inflammation. Additionally, L-Selectin knockout mice have relatively few lymphocytes present in peripheral lymph nodes and Peyer’s patches. Short-term in vivo homing experiments in L-Selectin deficient mice demonstrate that L-Selectin is involved in lymphocyte homing to Peyer’s patches and mesenteric lymph nodes in the gut. Rat and human L-Selectin share 77% amino acid sequence homology. Rat and mouse L-Selection share 83% amino acid sequence homology (1, 2).
L-selectin (CD62L antigen, Leukocyte surface antigen Leu-8) L-selectin is a member of the selectin family of glycoprotein adhesion and homing receptors that recognize sialyated carbohydrate groups and regulate lymphocyte-endothelial cell interactions. It is a type I transmembrane cell adhesion molecule (CAM) a... Read full blog post. |
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