Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to inhibit the adhesion of J45.01 human acute lymphoblastic leukemia T lymphocytes on immobilized JAM-2 (VE-JAM)/Fc Chimera. The ED50 for this effect is 0.1-0.5 µg/mL in the presence of 1 x 105 cells/well. Each well was coated with 100 µL of a 0.2 µg/mL solution of rhJAM-2 (VE-JAM)/Fc Chimera. |
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Source | Mouse myeloma cell line, NS0-derived mouse JAM-C protein
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Accession # | |||||||
N-terminal Sequence | Val32 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Jam3 |
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Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 50 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. |
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SDS-PAGE | 64 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
The family of junctional adhesion molecules (JAM), comprised of at least three members, are type I transmembrane receptors belonging to the immunoglobulin (Ig) superfamily (1, 2). These proteins are localized in the tight junctions between endothelial cells or epithelial cells. Some family members are also found on blood leukocytes and platelets. Mouse JAM-C cDNA predicts a 310 amino acid (aa) residue precursor protein with a putative 31 aa signal peptide, a 210 aa extracellular region containing two Ig domains, an 18 aa transmembrane domain and a 51 aa cytoplasmic domain containing a PDZ-binding motif and a PKC phosphorylation site (3). Mouse JAM-C shares 86% aa sequence identity with its human homologue. It also shares approximately 31% and 35% aa sequence homology with mouse JAM-A and JAM-B, respectively (2). Mouse JAM-C is highly expressed during embryogenesis. In adult tissues, mouse JAM-C is restricted to endothelial cells, lymph endothelial cells in the kidney, lymph node and Peyer’s patches where the protein can be localized to the high endothelial venules (3). Although human JAM-C is expressed on human platelets and a subset of leukocytes, mouse JAM-C expression was not detected on any mouse lymphocytes (4). In contrast to human JAM-C which show weak homotypic interactions, mouse JAM-C was reported to exhibit homotypic interactions (3). Mouse JAM-C has also been shown to have heterotypic interaction with JAM-B. It is likely that mouse JAM-C may play a role in lymphocyte transendothelial migration (4).
The nomenclature used for the JAM family proteins is confusing. VE-JAM has been referred to in the literature variously as JAM-B or JAM-C. Until further clarification, R&D Systems has adopted the nomenclature where both mouse and human VE-JAM are referred to as JAM-B.
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