Recombinant Human BCAM His-tag Protein, CF Summary
Product Specifications
Glu32-Ala547, 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.
11173-BC
Formulation | Supplied as a 0.2 μm filtered solution in PBS with Trehalose. |
Shipping | The product is shipped with dry ice or equivalent. 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 Human BCAM His-tag Protein (Catalog # 11173-BC) supports the adhesion TE‑85 human osteogenic sarcoma cells. The ED50 for this effect is 0.250-3.00 µg/mL.
2 μg/lane of Recombinant Human BCAM His-tag Protein (Catalog # 11173-BC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 67-82 kDa.
Reconstitution Calculator
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). Lu and BCAM differ by a 40 amino acid (aa) SH3-containing segment that is present in the cytoplasmic domain of Lutheran (1). Mature human BCAM consists of an extracellular domain (ECD) with two Ig-like V-type domains and three Ig-like C2-type domains, a transmembrane domain, and a short cytoplasmic domain (2,3). Within the ECD, human BCAM shares 73% amino acid (aa) identity with mouse and rat BCAM. A polymorphism at position 77 within the ECD is the basis for the difference between the Lua and Lub Lutheran blood groups (4). 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 (5-7). BCAM is also expressed on vascular and visceral smooth muscle cells and at the neuromuscular junction of skeletal muscle (6,8,9). Lu/BCAM binds to laminin, specifically isoforms containing the alpha 5 chain, which are found in basement membranes and are involved in cell differentiation, adhesion, migration, and proliferation (10). Overexpression of both BCAM and Lu on sickle red blood cells (SS RBC) has been found to play a role in vaso-occlusive crisis in sickle cell patients by contributing to the adhesion of erythrocytes to the vascular wall (11,12). The adhesive role of Lu/BCAM has been studied in the context of many diseases, including sickle cell disease, hereditary spherocytosis, myeloproliferative neoplasms and Gaucher disease (13). BCAM is upregulated on carcinomas, sarcomas, astrocytomas, and melanomas (14). Additionally, Lu/BCAM has been found to assist tumor cell migration via regulation of integrin-mediated cell attachment to laminin-511 (15).
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