CD31/PECAM-1 Antibody (TLD-3A12) [PE]

Cluster of differentiation (CD31), Platelet Endothelial Cell Adhesion Molecule 1 (PECAM-1), is a 30kDa type I transmembrane glycoprotein expressed by endothelial cells, platelets, leukocytes and some lymphocytes (e.g., B and T-cell subsets). Structurally, PECAM-1 consists of six extracellular immunoglobulin-like domains which serve to support various functions including homophilic binding, maintaining high expression of PECAM-1 within endothelial intercellular junctions, and supporting endothelial cell migration (1,2). PECAM's homophilic binding underscores its role in vascular barrier integrity and leukocyte trans-endothelial movement. However, PECAM may also engage in heterophilic interactions with molecules such as glycosaminoglycans (GAG), integrin alpha 5 beta 3, CD38 in lymphocytes and CD177/PR3 in neutrophils (2).

PECAM's intracellular cytoplasmic domain consists of a sequence of 118 amino acids and contains serine and tyrosine (also referred to as immunoreceptor tyrosine-based inhibitory motifs-ITIMs) residues, which may be phosphorylated upon cellular stimulation (3). ITIMs are phosphorylated by Src-family kinases and non-Src family kinases (e.g., Csk), leading to a conformational change which supports interactions with Src homology 2 (SH2) domain containing proteins such as protein-tyrosine phosphatase, SHP-2 (1,2). Formation of SHP-2/PECAM-1 complexes induces endothelial cell migration through the dephosphorylation of focal adhesion kinase and regulation of RhoA activity (1). Signaling downstream of ITIM tyrosine phosphorylations also plays a role in PECAM's anti-apoptotic activity, a function which is independent of its interaction with SHP-2. In platelets and leukocytes, phosphorylation of PECAM's cytosolic domain is inhibitory, preventing their activation.

References

1. Lertkiatmongkol, P., Liao, D., Mei, H., Hu, Y., & Newman, P. J. (2016). Endothelial functions of PECAM-1 (CD31). Current Opinion in Hematology. https://doi.org/10.1097/MOH.0000000000000239.Endothelial

2. Privratsky, J. R., & Newman, P. J. (2014). PECAM-1: Regulator of endothelial junctional integrity. Cell and Tissue Research. https://doi.org/10.1007/s00441-013-1779-3

3. Newman, P. J., & Newman, D. K. (2003). Signal transduction pathways mediated by PECAM-1: New roles for an old molecule in platelet and vascular cell biology. Arteriosclerosis, Thrombosis, and Vascular Biology. https://doi.org/10.1161/01.ATV.0000071347.69358.D9

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 1 confirmed species: Rat.

We have publications tested in 1 application: FLOW.

Showing Publication 1 - 1 of 1.

Publication using NB100-63704	Applications	Species
Zhou J, Rogers J, Lee S et al. Oral mucosa harbors a high frequency of endothelial cells - a novel postnatal cell source for angiogenic regeneration. Stem Cells Dev. 2016-11-10 [PMID: 27832737] (FLOW, Rat) Details: This citation used the DyLight 488 version of this antibody.	FLOW	Rat

Array NB100-63704

• CD31/PECAM-1 Antibodies
• CD31/PECAM-1 Antibody Pair
• CD31/PECAM-1 ELISA Kits
• CD31/PECAM-1 Lysate
• CD31/PECAM-1 Protein
• CD31/PECAM-1 Proteins and Enzymes
• CD31/PECAM-1 ELISAs