Recombinant Mouse BCAM Fc Chimera Protein, CF Summary
Product Specifications
Optimal dilutions should be determined by each laboratory for each application.
Mouse BCAM (Met1-Ala541) Accession # Q9R069 |
IEGRMDP | Mouse IgG2A (Glu98-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
7390-BC
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in 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.
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Reconstitution Calculator
Background: BCAM
Mouse Basal Cell Adhesion Molecule (BCAM), also known as CD239, is a member of immunoglobulin superfamily protein. In human, BCAM is the short splice form of the Lutheran blood group glycoprotein (Lu). Mature mouse BCAM consists of a 516 amino acid (aa) extracellular domain (ECD) with two Ig-like V-type domains and three Ig-like C2-type domains, a 21 aa transmembrane segment, and a 60 aa cytoplasmic domain (1). 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). BCAM is up‑regulated on carcinomas (particularly ovarian), sarcomas, astrocytomas, and melanomas (2, 3, 5, 6). 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). 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).
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