Recombinant Human BCAM Fc Chimera Protein, CF Summary
Optimal dilutions should be determined by each laboratory for each application.
(Glu32 - Ala547)
Accession # CAA58449
(Pro100 - Lys330)
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|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.
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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- 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.
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- Nishimune, H. et al. (2008) J. Cell Biol. 182:1201.
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- Rahuel, C. et al. (1999) Immunogenetics 50:271.
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- Wautier, M.-P. et al. (2007) Blood 110:894.
- Udani, M. et al. (1998) J. Clin. Invest. 101:2550.
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Citation for Recombinant Human BCAM Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Lutheran/basal cell adhesion molecule accelerates progression of crescentic glomerulonephritis in mice.
Authors: Huang J, Filipe A, Rahuel C, Bonnin P, Mesnard L, Guerin C, Wang Y, Le Van Kim C, Colin Y, Tharaux P
Kidney Int, 2014;85(5):1123-36.
Sample Types: Whole Blood
Applications: Adhesion Assay
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