Recombinant Mouse BCAM His-tag Protein, CF

Recombinant Mouse BCAM His-tag Protein (Catalog # 11174-BC) supports the adhesion of TE‑85 human osteogenic sarcoma cells. The ED50 for this effect is 18.0-162 ng/mL.

2 μg/lane of Recombinant Mouse BCAM His-tag Protein (Catalog # 11174-BC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 65-85 kDa.

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

Recombinant Mouse BCAM His-tag 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. The ED₅₀ for this effect is 18.0-162 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse BCAM protein
  Glu26-Ala541, with a C-terminal 6-His tag
• Accession #: Q9R069.1
• N-terminal Sequence: Glu26
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 58 kDa.
  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: 65-85 kDa, under 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 with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse BCAM His-tag 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

Background

Basal Cell Adhesion Molecule (BCAM), also known as CD239, is a member of immunoglobulin superfamily protein. BCAM arises from alternate splicing of the Lutheran blood group molecule (Lu) and lacks a 40 amino acid (aa) SH3-containing segment that is present in the cytoplasmic domain of Lutheran (1). Mature mouse BCAM consists of two Ig-like V-type domains and three Ig-like C2-type domains in the extracellular domain (ECD), a transmembrane segment, and a short cytoplasmic domain. 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). 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). BCAM is up‑regulated on carcinomas (particularly ovarian), sarcomas, astrocytomas, and melanomas (2, 3, 5, 6). 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.

Bioinformatics

• Uniprot:
  • Q9R069.1()