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Recombinant Human BCAM Fc Chimera Protein, CF

Bio-Techne includes R&D Systems | Catalog # 148-BC

Catalog #
Size / Price

Key Product Details



Accession #

Structure / Form

Disulfide-linked homodimer





Product Specifications


Mouse myeloma cell line, NS0-derived human BCAM protein
Human BCAM
(Glu32 - Ala547)
Accession # CAA58449
(Pro100 - Lys330)
6-His tag
N-terminus C-terminus


>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis


Predicted Molecular Mass

83.7 kDa (monomer)


110-120 kDa, reducing conditions


Measured by the ability of the immobilized protein to support the adhesion of TE‑85 human osteogenic sarcoma cells.
When 5 x 104 cells/well are added to human BCAM/Fc Chimera coated plates (25 µg/mL with 100 µL/well), approximately 40-80% will adhere after 1 hour incubation at 37 °C.
Optimal dilutions should be determined by each laboratory for each application.

Formulation, Preparation and Storage

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: BCAM

Human Basal Cell Adhesion Molecule (BCAM), also known as CD239, is an immunoglobulin superfamily protein that arises from alternate splicing of the Lutheran blood group molecule (Lu). BCAM lacks a 40 amino acid (aa) SH3-containing segment that is present in the cytoplasmic domain of Lutheran (1). The two isoforms are expressed as 85 kDa and 78 kDa glycoproteins (2 - 4). A polymorphism at position 77 within the extracellular domain (ECD) of human BCAM is the basis for the difference between the Lua and Lub Lutheran blood groups (5). The ECD of human BCAM contains two Ig-like V-type domains and three Ig-like C2-type domains (5, 6). It shares 73% aa sequence identity with the ECDs of mouse and rat BCAM. 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 (3, 7 - 9). On polarized epithelium, the Lutheran isoform is restricted to the basolateral membrane, while the short isoform is also found on the apical face (2). In the superficial layer of stratified epithelium, however, it shows a nonpolarized distribution (3). BCAM is also expressed on vascular and visceral smooth muscle cells and at the neuromuscular junction of skeletal muscle (3, 8, 10, 11). BCAM is upregulated on carcinomas (particularly ovarian), sarcomas, astrocytomas, and melanomas (3, 7, 9, 10). It cooperates with Integrins beta1 and alphaV beta3 as an adhesion receptor for Laminins which contain the alpha5 chain (4, 12). Mouse BCAM binds to both human and mouse Laminin, whereas human BCAM binds to human but not to mouse Laminin (13). In contrast to mouse, human BCAM is additionally expressed on erythrocytes and is upregulated on these cells in sickle cell disease and polycythemia vera (8, 14, 15). It mediates increased binding of erythrocytes to Laminin and promotes the formation of erythrocyte-monocyte aggregates (8, 14 - 18). The Lutheran isoform is aberrantly phosphorylated in erythroid disorders and can enhance Laminin-mediated adhesion of erythrocytes to vascular endothelial cells (15, 18).


  1. Rahuel, C. et al. (1996) Blood 88:1865.
  2. El Nemer, W. et al. (1999) J. Biol. Chem. 274:31903.
  3. Garin-Chesa, P. et al. (1994) Int. J. Oncol. 5:1261.
  4. Vainionpaa, N. et al. (2006) Am. J. Physiol. Cell. Physiol. 290:C764.
  5. El Nemer, W. et al. (1997) Blood 89:4608.
  6. Campbell, I.G. et al. (1994) Cancer Res. 54:5761.
  7. Schon, M. et al. (2000) J. Invest. Dermatol. 115:1047.
  8. Rahuel, C. et al. (2008) Am. J. Physiol. Renal Physiol. 294:F393.
  9. Rettig, W.J. et al. (1986) Cancer Res. 46:6406.
  10. Rettig, W.J. et al. (1988) Proc. Natl. Acad. Sci. 85:3110.
  11. Nishimune, H. et al. (2008) J. Cell Biol. 182:1201.
  12. Kikkawa, Y. et al. (2007) J. Biol. Chem. 282:14853.
  13. Rahuel, C. et al. (1999) Immunogenetics 50:271.
  14. Zen, Q. et al. (1999) J. Biol. Chem. 274:728.
  15. Wautier, M.-P. et al. (2007) Blood 110:894.
  16. Udani, M. et al. (1998) J. Clin. Invest. 101:2550.
  17. Chaar, V. et al. (2010) Haematologica 95:1841.
  18. Gauthier, E. et al. (2009) Br. J. Haematol. 148:456.

Long Name

Basal Cell Adhesion Molecule

Alternate Names


Entrez Gene IDs

4059 (Human); 57278 (Mouse)

Gene Symbol



Additional BCAM Products

Product Documents for Recombinant Human BCAM Fc Chimera Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human BCAM Fc Chimera Protein, CF

For research use only

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