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

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

Product Specifications

>95%, by SDS-PAGE with silver staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
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.
Human embryonic kidney cell, HEK293-derived human CD31/PECAM-1 protein
Human CD31/PECAM-1
Accession # P16284
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained. Gln28 inferred from enzymatic pyroglutamate treatment revealing Glu29
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
91 kDa

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


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.
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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).

  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-1; platelet/endothelial cell adhesion molecule

Citation for Recombinant Human CD31/PECAM-1 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Endothelial E-selectin inhibition improves acute myeloid leukaemia therapy by disrupting vascular niche-mediated chemoresistance
    Authors: V Barbier, J Erbani, C Fiveash, JM Davies, J Tay, MR Tallack, J Lowe, JL Magnani, DR Pattabiram, AC Perkins, J Lisle, JEJ Rasko, JP Levesque, IG Winkler
    Nat Commun, 2020;11(1):2042.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay


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