Product nameAnti-CD31 antibody - C-terminal, prediluted
See all CD31 primary antibodies
DescriptionRabbit polyclonal to CD31 - C-terminal, prediluted
Tested applicationsSuitable for: IHC-Pmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Pig
Synthetic peptide corresponding to Mouse CD31 (C terminal).
Database link: P16284
- IHC-P: Human tonsil tissue.
For manual IHC only.
Storage instructionsShipped at 4°C. Store at +4°C. Do Not Freeze.
Storage bufferpH: 7.60
Preservative: 0.1% Sodium azide
Constituents: Tris buffered saline, 1% BSA
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab28365 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Ready to use.
Boil tissue section in Citrate buffer, pH 6.0 for 10 min followed by cooling at room temperature for 20 min.
Primary antibody incubation for 30 minutes at room temperature.
FunctionInduces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).
Tissue specificityExpressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells. Isoform Long predominates in all tissues examined. Isoform Delta12 is detected only in trachea. Isoform Delta14-15 is only detected in lung. Isoform Delta14 is detected in all tissues examined with the strongest expression in heart. Isoform Delta15 is expressed in brain, testis, ovary, cell surface of platelets, human umbilical vein endothelial cells (HUVECs), Jurkat T-cell leukemia, human erythroleukemia (HEL) and U937 histiocytic lymphoma cell lines (at protein level).
Sequence similaritiesContains 6 Ig-like C2-type (immunoglobulin-like) domains.
DomainThe Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity.
modificationsPhosphorylated on Ser and Tyr residues after cellular activation. In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation.
Cellular localizationMembrane. Cell junction. Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells and Cell junction. Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.
- Information by UniProt
- Adhesion molecule antibody
- CD31 antibody
- CD31 antigen antibody
This product has been referenced in:
- Zhao C et al. ETV2 mediates endothelial transdifferentiation of glioblastoma. Signal Transduct Target Ther 3:4 (2018). Read more (PubMed: 29527330) »
- Griveau A et al. A Glial Signature and Wnt7 Signaling Regulate Glioma-Vascular Interactions and Tumor Microenvironment. Cancer Cell 33:874-889.e7 (2018). Read more (PubMed: 29681511) »