>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
83.7 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
110-120 kDa, reducing conditions
Publications
Read Publications using 148-BC in the following applications:
Lutheran blood group (Auberger b antigen included)
Lutheran blood group glycoprotein
MSK19
Background
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).
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El Nemer, W. et al. (1999) J. Biol. Chem. 274:31903.
Garin-Chesa, P. et al. (1994) Int. J. Oncol. 5:1261.
Vainionpaa, N. et al. (2006) Am. J. Physiol. Cell. Physiol. 290:C764.
El Nemer, W. et al. (1997) Blood 89:4608.
Campbell, I.G. et al. (1994) Cancer Res. 54:5761.
Schon, M. et al. (2000) J. Invest. Dermatol. 115:1047.
Rahuel, C. et al. (2008) Am. J. Physiol. Renal Physiol. 294:F393.
Rettig, W.J. et al. (1986) Cancer Res. 46:6406.
Rettig, W.J. et al. (1988) Proc. Natl. Acad. Sci. 85:3110.
Nishimune, H. et al. (2008) J. Cell Biol. 182:1201.
Kikkawa, Y. et al. (2007) J. Biol. Chem. 282:14853.
Rahuel, C. et al. (1999) Immunogenetics 50:271.
Zen, Q. et al. (1999) J. Biol. Chem. 274:728.
Wautier, M.-P. et al. (2007) Blood 110:894.
Udani, M. et al. (1998) J. Clin. Invest. 101:2550.
Chaar, V. et al. (2010) Haematologica 95:1841.
Gauthier, E. et al. (2009) Br. J. Haematol. 148:456.
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