Recombinant Mouse BCAM His-tag Protein, CF Summary
Product Specifications
Glu26-Ala541, with a C-terminal 6-His tag
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.
11174-BC
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 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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Scientific Data
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.
Reconstitution Calculator
Background: BCAM
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).
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