Recombinant Mouse BCAM Fc Chimera Protein, CF


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Product Details

Reactivity MuSpecies Glossary
Applications Bioactivity

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Recombinant Mouse BCAM Fc Chimera Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of TE‑85 human osteogenic sarcoma cells. When 5 x 104 cells per well are added to Recombinant Mouse BCAM Fc Chimera coated plates, cell adhesion is enhanced in a dose dependent manner. The ED50 for this effect is 20‑100 ng/mL.
Optimal dilutions should be determined by each laboratory for each application.
Mouse myeloma cell line, NS0-derived mouse BCAM protein
Mouse BCAM
Accession # Q9R069
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>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.


Theoretical MW
84 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.
95‑105 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse BCAM Fc Chimera Protein, CF

  • antigen identified by monoclonal F8
  • Auberger B antigen
  • basal cell adhesion molecule (Lu and Au blood groups)
  • basal cell adhesion molecule (Lutheran blood group)
  • basal cell adhesion molecule
  • B-CAM cell surface glycoprotein
  • BCAM
  • B-cell adhesion molecule
  • CD239 antigen
  • CD239
  • F8/G253 antigen
  • glycoprotein 95kDa
  • LUAU
  • Lutheran antigen
  • Lutheran blood group (Auberger b antigen included)
  • Lutheran blood group glycoprotein
  • MSK19


Mouse Basal Cell Adhesion Molecule (BCAM), also known as CD239, is a member of immunoglobulin superfamily protein. In human, BCAM is the short splice form of the Lutheran blood group glycoprotein (Lu). Mature mouse BCAM consists of a 516 amino acid (aa) extracellular domain (ECD) with two Ig-like V-type domains and three Ig-like C2-type domains, a 21 aa transmembrane segment, and a 60 aa cytoplasmic domain (1). Within the ECD, mouse BCAM shares 73% and 91% aa sequence identity with human and rat BCAM, respectively. BCAM is widely expressed in epithelial and endothelial tissues including in the vasculature, kidney glomerulus, small intestine, colon, hair follicle outer root sheath, and basal keratinocytes of the skin during inflammation (2‑5). BCAM is also expressed on vascular and visceral smooth muscle cells and at the neuromuscular junction of skeletal muscle (2, 4, 6, 7). BCAM is up‑regulated on carcinomas (particularly ovarian), sarcomas, astrocytomas, and melanomas (2, 3, 5, 6). It cooperates with Integrins beta 1 and alpha V beta 3 as an adhesion receptor for Laminins which contain the alpha 5 chain (8, 9). Mouse BCAM binds to both human and mouse Laminin, whereas human BCAM binds to human but not to mouse Laminin (1). In contrast to mouse, human BCAM is additionally expressed on erythrocytes and is up‑regulated on these cells in sickle cell disease and polycythemia vera (4, 10, 11). In human erythroid disorders, it mediates increased binding of erythrocytes to Laminin and promotes the formation of erythrocyte-monocyte aggregates (4, 10‑14).
  1. Rahuel, C. et al. (1999) Immunogenetics 50:271.
  2. Garin-Chesa, P. et al. (1994) Int. J. Oncol. 5:1261.
  3. Schon, M. et al. (2000) J. Invest. Dermatol. 115:1047.
  4. Rahuel, C. et al. (2008) Am. J. Physiol. Renal Physiol. 294:F393.
  5. Rettig, W.J. et al. (1986) Cancer Res. 46:6406.
  6. Rettig, W.J. et al. (1988) Proc. Natl. Acad. Sci. 85:3110.
  7. Nishimune, H. et al. (2008) J. Cell Biol. 182:1201.
  8. Kikkawa, Y. et al. (2007) J. Biol. Chem. 282:14853.
  9. Vainionpaa, N. et al. (2006) Am. J. Physiol. Cell. Physiol. 290:C764.
  10. Zen, Q. et al. (1999) J. Biol. Chem. 274:728.
  11. Wautier, M.-P. et al. (2007) Blood 110:894.
  12. Udani, M. et al. (1998) J. Clin. Invest. 101:2550.
  13. Chaar, V. et al. (2010) Haematologica 95:1841.
  14. Gauthier, E. et al. (2009) Br. J. Haematol. 148:456.

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