Recombinant Human BCAM Fc Chimera Protein, CF

R&D Systems | Catalog # 148-BC

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Key Product Details

  • R&D Systems NS0-derived Recombinant Human BCAM Fc Chimera Protein (148-BC)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

CAA58449

Structure / Form

Disulfide-linked homodimer

Applications

Bioactivity
View all BCAM Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human BCAM protein
Human BCAM
(Glu32 - Ala547)
Accession # CAA58449		 DIEGRMD Human IgG1
(Pro100 - Lys330)		 6-His tag
N-terminus C-terminus

Purity

>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

Glu32

Predicted Molecular Mass

83.7 kDa (monomer)

SDS-PAGE

110-120 kDa, reducing conditions

Activity

Bioassay data are not available.

Formulation, Preparation, and Storage

148-BC
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution

Reconstitute at 100 μg/mL in sterile PBS.
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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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 beta 1 and alpha V beta 3 as an adhesion receptor for Laminins which contain the alpha 5 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).

References

  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

CD239

Entrez Gene IDs

4059 (Human); 57278 (Mouse)

Gene Symbol

BCAM

UniProt

CAA58449

Additional BCAM Products

Product Documents for Recombinant Human BCAM Fc Chimera Protein, CF

Certificate of Analysis

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

For research use only

Citations for Recombinant Human BCAM Fc Chimera Protein, CF

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