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PSGL-1/CD162  Protein, Antibody, ELISA Kit, cDNA Clone

表達宿主: Human Cells  
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13863-H08H-50
13863-H08H-100
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100 µg 
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表達宿主: Human Cells  
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10490-H03H-50
10490-H03H-100
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100 µg 
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表達宿主: Human Cells  
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50770-M02H-50
50770-M02H-100
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100 µg 
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表達宿主: Human Cells  
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50770-MCCH-50
50770-MCCH-100
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100 µg 
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PSGL-1/CD162 相关研究领域

PSGL-1/CD162 相關信號通路

    PSGL-1/CD162 概述&蛋白信息

    PSGL-1/CD162 研究背景

    基因概述: SELPLG gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of SELPLG gene and polymorphisms in SELPLG gene are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Apr 2011]
    General information above from NCBI
    亞單位結構: Homodimer; disulfide-linked. Interaction with P-, E- and L-selectins, through their lectin/EGF domains, is required for promoting recruitment and rolling of leukocytes. These interactions require sialyl Lewis X glycan modification but there is a differing dependence for tyrosine sulfations. Sulfation on Tyr-51 of PSGL1 is most important for high affinity L-selectin/SELL binding while P-selectin/SELP requires sulfation on Tyr-48. E-selectin/SELE binds with much lower affinity and requires the sLe(x) epitope, but apparantly not tyrosine sulfation. Dimerization appears not to be required for P-selectin/SELP binding. Interacts with SNX20. Interacts with MSN and SYK; mediates the activation of SYK by SELPLG. {ECO:0000269|PubMed:10713099, ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:11566773, ECO:0000269|PubMed:12387735, ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:12736247, ECO:0000269|PubMed:18196517, ECO:0000269|PubMed:7521878, ECO:0000269|PubMed:7559387, ECO:0000269|PubMed:7585949, ECO:0000269|PubMed:7585950}.
    亞細胞定位: Membrane; Single-pass type I membrane protein.
    組織特異性: Expressed on neutrophils, monocytes and most lymphocytes.
    翻譯後修飾: Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning in leukocyte rolling. The modification containing the sialyl Lewis X glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation. {ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:12736247}.; Sulfation, in conjunction with the SLe(x)-containing glycan, is necessary for P- and L-selectin binding. High affinity P-selectin binding has a preferred requirement for the isomer sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. These sulfations play an important role in L- and P-selectin-mediated neutrophil recruitment, and leukocyte rolling. {ECO:0000269|PubMed:11081633}.

    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.

    PSGL-1/CD162 別稱

    PSGL-1/CD162 相關文獻

    1. Sako, D. et al., 1993, Cell. 75: 1179-1186.

    2. Wilkins, P. P. et al., 1995, J. Biol. Chem. 270: 22677-22680.

    3. Frenette, P. S. et al., 2000, J. Exp. Med. 191: 1413-1422.

    4. Vandendries, E.R .et al., 2004, Thromb. Haemost. 92: 459-466..

    5. Pouyani, T. et al., 1995, Cell. 83: 333-343.

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