|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A polyhistidine-tag is an amino acid motif in proteins that consists of at least five histidine (His) residues, often at the N- or C-terminus of the protein.
Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems.
|Mouse SELPLG ORF mammalian expression plasmid, C-GFPSpark tag||MG50770-ACG|
|Mouse SELPLG ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50770-ACR|
|Mouse SELPLG ORF mammalian expression plasmid, C-Flag tag||MG50770-CF|
|Mouse SELPLG ORF mammalian expression plasmid, C-His tag||MG50770-CH|
|Mouse SELPLG ORF mammalian expression plasmid, C-Myc tag||MG50770-CM|
|Mouse SELPLG ORF mammalian expression plasmid, C-HA tag||MG50770-CY|
|Mouse SELPLG Gene cDNA clone plasmid||MG50770-G|
|Mouse SELPLG ORF mammalian expression plasmid, N-Flag tag||MG50770-NF|
|Mouse SELPLG ORF mammalian expression plasmid, N-His tag||MG50770-NH|
|Mouse SELPLG ORF mammalian expression plasmid, N-Myc tag||MG50770-NM|
|Mouse SELPLG ORF mammalian expression plasmid, N-HA tag||MG50770-NY|
|Mouse SELPLG natural ORF mammalian expression plasmid||MG50770-UT|
|Learn more about expression Vectors|
P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinitycounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. PSGL-1 is a mucin-type glycoprotein, expressed on leukocytes and platelets as a homodimer of two disulfide-linked subunits of ~120 kD. As cell adhesion molecules, multiple studies have shown that PSGL-1/ P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 protein requires two distinct posttranslational modifications for the Ca2+-dependent recognition by the lectin domain of P-selectin, that is tyrosine sulfation and specific O-linked glycosylation (sialic acid and fucose). PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.
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