Recombinant Human CD31/PECAM-1 Fc Chimera Protein, CF 50 UG

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Recombinant Human CD31/PECAM-1 Fc Chimera Protein, CF 50 UG信息二维码

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产品介绍

    基本参数

    详细说明

    • Purity

      >95%, by SDS-PAGE with silver staining

    • Endotoxin Level

      <0.10 EU per 1 μg of the protein by the LAL method.  

    • Activity

      Measured by the ability of the immobilized protein to support the adhesion of HUVEC human umbilical vein endothelial cells. Bird, I.N.     et al. (1999) J. Cell Sci.     112:1989. The ED50 for this effect is 1-6 μg/mL.    
       

    • Source

      Human embryonic kidney cell, HEK293-derived

      Human CD31/PECAM-1
      (Gln28-Lys600)
      Accession # P16284
      IEGRMDHuman IgG1
      (Pro100-Lys330)
      N-terminus
      C-terminus
    • N-terminal Sequence    
      Analysis

      No results obtained. Gln28 inferred from enzymatic pyroglutamate treatment revealing Glu29

    • Structure / Form

      Disulfide-linked homodimer

    • Predicted Molecular Mass

      91 kDa

    8636-PC

     

    Formulation Lyophilized from a 0.2 μm filtered solution in PBS and Trehalose.


    Reconstitution Reconstitute at 500 μg/mL in PBS.



    Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.


    Stability & Storage:       Use a manual defrost freezer and avoid repeated freeze-thaw cycles.      

    • 12 months from date of receipt, -20 to -70 °C as supplied.

    • 1 month, 2 to 8 °C under sterile conditions after reconstitution.

    • 3 months, -20 to -70 °C under sterile conditions after reconstitution.


    Background: CD31/PECAM-1

    CD31, also known as platelet endothelial cell adhesion molecule-1 (PECAM-1), is a 130 kDa heavily glycosylated transmembrane protein belonging to the immunoglobulin (Ig) superfamily of cell adhesion molecules (1, 2). CD31 is highly expressed on endothelial cells and at a lower level on platelets, granulocytes, macrophages, dendritic cells, T and B cells, and natural killer (NK) cells. It is involved in cell adhesion and is required for transepithelial migration of leukocytes (TEM) (3, 4). CD31 is composed of an extracellular domain (ECD) of 574 amino acids (aa) containing six Ig-like domains, a transmembrane domain, and a 118 aa cytoplasmic domain (5). The latter undergoes alternative splicing which generates multiple isoforms showing altered adhesive properties compared to full length CD31 (6). The human CD31 ECD shares 63% and 61% aa sequence identity with mouse and rat CD31, respectively. CD31 acts as a homophilic receptor through its extracellular domain and is involved in downstream signaling via its cytoplasmic domain (7). This domain contains highly conserved ITIM motifs which, once tyrosine phosphorylated, recruit and activate the signaling molecules Src and SHP-2 (1, 8). The resulting inhibition of TCR signaling increases the activation threshold of T cells, thus reinforcing peripheral tolerance and preventing development of autoimmunity (9). CD31 additionally regulates immune responses by acting as a key inhibitory receptor in dendritic cell development (10). Besides its role in TEM, CD31 appears to regulate T cell trafficking through a complex coordination of endothelial cell junctions and T cell extravasation (11). In vitro, a 110 kDa soluble form of CD31 is released following shedding of the extracellular domain during endothelial cell apoptosis (12). This ectodomain has also been identified in the serum of patients suffering from myocardial infarction, acute ischaemic stroke, and multiple sclerosis, conditions that involve tissue damage and endothelial cell apoptosis (13-15).

    • References:

      1. Ilan, N. and J.A. Madri (2003) Curr. Opin. Cell Biol. 15:515.

      2. Xie, Y. and W.A. Muller (1993) Proc. Natl. Acad. Sci. USA 90:5569.

      3. Thompson, R.D. et al. (2000) J. Immunol. 165:426.

      4. Schenkel, A.R. et al. (2004) J. Immunol. 173:6403.

      5. Newman, P.J. et al. (1990) Science 247:1219.

      6. Yan, H.C. et al. (1995) J. Biol. Chem. 270:23672.

      7. Newton, J.P. et al. (1997) J. Biol. Chem. 272:20555.

      8. Osawa, M. et al. (2002) J. Cell Biol. 158:773.

      9. Marelli-Berg, F.M. et al. (2013) J. Cell Sci. 126:2343.

      10. Clement, M. et al. (2014) Proc. Natl. Acad. Sci. USA 111:E1101.

      11. Ma, L. et al. (2012) J. Immunol. 189:4104.

      12. Ilan, N. et al. (2001) FASEB J. 15:362.

      13. Serebruany, V.L. et al. (1999) Cardiology 91:50.

      14. Zaremba, J. and J. Losy (2002) Acta. Neurol. Scand. 106:292.

      15. Losy, J. et al. (1999) J. Neuroimmunol. 99:169.

    • Long Name:

      Platelet Endothelial Cell Adhesion Molecule 1

    • Entrez Gene IDs:

      5175 (Human); 18613 (Mouse); 29583 (Rat)

    • Alternate Names:

      adhesion molecule; CD31 antigen; CD31; CD31/EndoCAM; endoCAM; FLJ34100; FLJ58394; GPIIA'; PECA1; PECAM1; PECAM-1; PECAM-1, CD31/EndoCAM; platelet endothelial cell adhesion molecule; platelet/endothelial cell adhesion molecule














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