Measured by its binding ability in a functional ELISA. Recombinant Mouse CD31/PECAM-1 (Catalog # 3628-PC) binds to Recombinant Human Integrin alpha 8 beta 1 with an ED 50 of 0.060-0.720 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse CD31/PECAM-1 protein Glu18-Lys590, with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
65.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
91-100 kDa, reducing conditions
Publications
Read Publications using 3628-PC in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse CD31/PECAM-1 Protein, CF
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
Background
PECAM-1 (platelet-endothelial cell adhesion molecule-1; also known as CD31) is a 130 kDa type I transmembrane glycoprotein adhesion molecule in the immunoglobulin superfamily (1, 2). Expression is restricted to cells involved in circulation, especially endothelial cells, platelets, monocytes, neutrophils and lymphocyte subsets. PECAM-1 is concentrated at cell-cell junctions and is required for transendothelial migration (TEM) (1 - 3). The extracellular domain (ECD) of PECAM-1 has ten potential N-linked glycosylation sites and six C2-type Ig-like domains, the first of which is critical for adhesion and extravasation (3, 4). The cytoplasmic domain contains immunoregulatory tyrosine-based inhibitory and switch motifs (ITIM, ITSM) that mediate both inhibition and activation via phosphotyrosine-mediated engagement of SH2-containing signaling molecules (1, 5). Metalloproteinase-mediated ectodomain shedding occurs during apoptosis (6) but increased serum PECAM-1 ectodomain in HIV and active multiple sclerosis occurs independent of apoptosis (7, 8). In humans, expression of six isoforms with exon deletions in the cytoplasmic domain is tissue- and stage-specific, but full-length PECAM-1 is predominant. A form lacking the ITSM predominates in mouse (9). Mouse PECAM-1 ECD shows 77%, 63%, 63%, 63% and 61% amino acid (aa) identity with rat, human, canine, porcine and bovine PECAM-1, respectively. PECAM-1 participates with other adhesion molecules in some functions, but is the critical molecule for TEM. Homotypic PECAM-1 adhesion in trans, combined with cycling of PECAM-1 to and from surface-connected endothelial cell vesicles, leads leukocytes across endothelial tight junctions (3, 10). Homotypic adhesion and signaling functions also strongly suppress mitochondria-dependent apoptosis (11). In platelets, PECAM-1 is necessary for limiting thrombus formation (12) and promoting integrin-mediated clot retraction and platelet spreading (13), but mechanisms for these phenomena are unclear. PECAM -/- mice are deficient in chemokine-mediated chemotaxis (14).
Ilan, N. and J.A. Madri (2003) Curr. Opin. Cell Biol. 15:515.
Xie, Y. and Muller, W.A. (1993) Proc. Natl. Acad. Sci. USA 90:5569.
Liao, F. et al. (1997) J. Exp. Med. 185:1349.
Nakada, M.T. et al. (2000) J. Immunol. 164:452.
Chemnitz, J.M. et al. (2004) J. Immunol. 173:945.
Ilan, N. et al. (2001) FASEB J. 15:362.
Eugenin, E.A. et al. (2006) J. Leukoc. Biol. 79:444.
Losy, J. et al. (1999) J. Neuroimmunol. 99:169.
Wang, Y. et al. (2003) Am. J. Physiol. Heart Circ. Physiol. 284:H1008.
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