Recombinant Human JAM-A Fc Chimera Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human JAM-A Fc Chimera Protein, CF Summary

• Details of Functionality: Bioassay data are not available.
• Source: Mouse myeloma cell line, NS0-derived human JAM-A protein
  

  Human JAM-A (Ser28 - Ala242) Accession # Q9Y624	IEGRMD	Human IgG1 (Pro100 - Lys330)
  N-terminus		C-terminus

• Accession #: Q9Y624
• N-terminal Sequence: Ser28
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: F11R
• Purity: >90%, 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: 60-65 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: 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: >90%, 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 Human JAM-A Fc Chimera Protein, CF

• CD321 antigen
• CD321
• F11 receptor
• F11R
• JAM-1
• JAM1CD321
• JAMA
• JAM-A
• JCAMJAM
• Junctional adhesion molecule 1Platelet F11 receptor
• junctional adhesion molecule A
• PAM-1
• PAM-1KAT
• Platelet adhesion molecule 1

Background

The family of junctional 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 or epithelial cells. Some family members are also found on blood leukocytes and platelets. Human JAM-A, also known as platelet adhesion molecule 1 (PAM-1) and platelet F11 receptor (3), is predominantly expressed at intercellular junctions of both epithelial cells and endothelial cells (1 - 4). It is also expressed on circulating blood cells including neutrophils, monocytes, platelets, erythrocytes and lymphocytes (5). Human JAM-A cDNA predicts a 299 amino acid (aa) residue precursor protein with a putative 27 aa signal peptide, a 210 aa extracellular region containing two Ig-like V-subset domains, a 24 aa transmembrane domain and a 38 aa cytoplasmic domain. The human and mouse proteins share approximately 67% aa sequence homology. Human JAM-A also shares approximately 35% and 32% aa sequence homology with human JAM-B and JAM-C, respectively. JAM-A exhibits homophilic interactions to regulate tight junction assembly and modulate paracellular permeability. This homophilic interation also mediates platelet aggregation and adhesion to endothelial cells and may play a role in thrombosis (3). JAM-A binds heterotypically with the beta 2 integrin lymphocyte function-associated antigen-1 (LFA-1). This JAM-A-LFA-1 interaction is involved in leukocyte adhesion and transmigration (6). JAM-A has also been shown to bind reovirus attachment protein sigma-1 to permit reovirus infection and signal virus-induced apoptosis (7).

1. Chavakis, T. et al. (2003) Thromb. Haemost. 89:13.
2. Aurand-Lions, M. et al. (2001) Blood 98:3699.
3. Sobocka, M.B. et al. (2000) Blood 95:2600.
4. Martin-Padura, I. et al. (1998) J. Cell Biol. 142:117.
5. Williams, L.A. et. al. (1999) Mol. Immunol. 36:1175.
6. Ostermann, G. et al. (2002) Nature Immunol. 3:151.
7. Barton, E.S. et al. (2001) Cell 104:441.

Publications for JAM-A (1103-JM)(5)

Publications using 1103-JM

• E Walker, SM Turaga, X Wang, R Gopalakris, S Shukla, JP Basilion, JD Lathia Development of near-infrared imaging agents for detection of junction adhesion molecule-A protein Translational Oncology, 2021;14(3):101007. 2021 [PMID: 33421750] (Bioassay, Human)
• Williams D, Anastos K, Morgello S, Berman J JAM-A and ALCAM are therapeutic targets to inhibit diapedesis across the BBB of CD14+CD16+ monocytes in HIV-infected individuals. J Leukoc Biol, 2015;97(2):401-12. 2015 [PMID: 25420915] (Standard, Human)
• Haarmann A, Deiss A, Prochaska J, Foerch C, Weksler B, Romero I, Couraud PO, Stoll G, Rieckmann P, Buttmann M Evaluation of soluble junctional adhesion molecule-A as a biomarker of human brain endothelial barrier breakdown. PLoS ONE, 2010;5(10):e13568. 2010 [PMID: 21060661] (ELISA (Standard), N/A)
• Miljkovic-Licina M, Hammel P, Garrido-Urbani S, Bradfield PF, Szepetowski P, Imhof BA Sushi repeat protein X-linked 2, a novel mediator of angiogenesis. FASEB J., 2009;23(12):4105-16. 2009 [PMID: 19667118] (Immunoprecipitation, Mouse)
• Koenen RR, Pruessmeyer J, Soehnlein O, Fraemohs L, Zernecke A, Schwarz N, Reiss K, Sarabi A, Lindbom L, Hackeng TM, Weber C, Ludwig A Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases. Blood, 2009;113(19):4799-809. 2009 [PMID: 19258599] (Enzyme Assay, Human)

Bioinformatics

• Gene Symbol: F11R
• Uniprot:
  • Q9Y624()