Recombinant Mouse JAM-B/VE-JAM Fc Chimera Protein, CF Summary
Details of Functionality
Measured by the ability of the immobilized protein to support adhesion of J45.01 human acute lymphoblastic leukemia T lymphocytes. Liang, T.W. et al. (2002) J. Immunol. 168:1618.
When Recombinant Mouse JAM-B Fc Chimera is immobilized on goat anti-human IgG Fc antibody coated wells, J45.01 cells (100 µL/well at 106 cells/mL) adhesion is induced in a dose dependent manner after a 2 hour incubation at 37 °C. The ED50 for this effect is 10-60 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse JAM-B/VE-JAM protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
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.
SDS-PAGE
64-70 kDa, reducing conditions
Publications
Read Publications using 988-VJ in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 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 JAM-B/VE-JAM Fc Chimera Protein, CF
C21orf43
CD322 antigen
CD322
JAM2
JAMB
JAM-B
JAM-BJAM-IT/VE-JAM
junctional adhesion molecule 2JAM-2
junctional adhesion molecule B
PRO245
Vascular endothelial junction-associated molecule
VE-JAM
VE-JAMVEJAMCD322
Background
The family of juctional adhesion molecules (JAM), comprising 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. JAM-B, alternatively named vascular endothelial JAM (VE-JAM), is expressed prominently on high endothelial venules of lymphoid organs where it is localized to the intercellular boundaries of high endothelial cells. It is also expressed on the endothelium of a variety of non-lymphoid organs, especially the heart and placenta (2, 3, 5). Mouse JAM-B/VE-JAM cDNA predicts a 298 amino acid (aa) residue precursor protein with a putative 28 aa signal peptide, a 209 aa extracellular region containing two Ig domains, a 23 aa transmembrane domain and a 38 aa cytoplasmic domain containing a PDZ-binding motif and a PKC phosphorylation site (2, 3). Mouse JAM-B shares approximately 79% aa sequence homology with its human homologue. It also shares approximately 35% aa sequence homology with mouse JAM-A or JAM-C. JAM-B exhibits homotypic interactions, as well as heterotypic interactions with JAM-C, but not JAM-A (4, 5, 7). It is also a ligand for the integrin alpha4beta1. However, the JAM‑B/alpha4beta1 interaction is facilitated only after prior adhesion of JAM-B to JAM-C (6). Through its heterotypic interactions with JAM-C, JAM-B is an adhesive ligand for T, NK, and dendritic cells, and may play a role in regulating leukocyte transmigration (5).
Chavakis, T. et al. (2003) Thromb. Haemost. 89:13.
Aurand-Lions, M. et al. (2001) Blood 98:3699.
Palmeri, A. et al. (2000) J. Biol. Chem. 275:19139.
Cunnigham, S. et al. (2000) J. Biol. Chem. 275:34750.
Liang, T. et al. (2002) J. Immunol. 168:1618.
Cunningham, A. et al. (2002) J Biol. Chem. 277:27589.
Arrate, M. et al. (2001) J. Biol. Chem. 276:45826.
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