Recombinant Human BCAM His-tag Protein, CF

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.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human BCAM His-tag Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of TE‑85 human osteogenic sarcoma cells. The ED₅₀ for this effect is 0.250-3.00 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human BCAM protein
  Glu32-Ala547, with a C-terminal 6-His tag
• Accession #: CAA58449.1
• N-terminal Sequence: Glu32
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 57 kDa.
  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: 67-82 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human BCAM His-tag Protein, CF

• antigen identified by monoclonal F8
• Auberger B antigen
• basal cell adhesion molecule (Lu and Au blood groups)
• basal cell adhesion molecule (Lutheran blood group)
• basal cell adhesion molecule
• B-CAM cell surface glycoprotein
• BCAM
• B-cell adhesion molecule
• CD239 antigen
• CD239
• F8/G253 antigen
• glycoprotein 95kDa
• LUAU
• Lutheran antigen
• 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). 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).

1. Rahuel, C. et al. (1996) Blood 88:1865.
2. Vainionpaa, N. et al. (2006) Am. J. Physiol. Cell Physiol. 290:C764.
3. El Nemer, W. et al. (1997) Blood 89:4608.
4. El Nemer, W. et al. (1999) J. Biol. Chem. 274:31903.
5. Schon, M. et al. (2000) J. Invest. Dermatol. 115:1047.
6. Rahuel, C. et al. (2008) Am. J. Physiol. Renal Physiol. 294:F393.
7. Rettig, W.J. et al. (1986) Cancer Res. 46:6406.
8. Nishimune, H. et al. (2008) J. Cell Biol. 182:1201.
9. Kikkawa, Y. et al. (2007) J. Biol. Chem. 282:14853.
10. El Nemer, W. et al. (2001) J Biol Chem 276:23757.
11. Eyler, C.E. and Telen, M.J. (2006) Transfusion. 46(4).
12. Klei, TRL. et al. (2018) Blood Adv. 2:14.
13. Guadall, A. et al. (2019). J. Biol. Chem. 294:14911.
14. Chang, H.Y. et al. (2017) J. Biomed Sci 24:61.
15. Kikkawa, Y. et al. (2013) J. Biol. Chem. 288:30990.

Bioinformatics

• Uniprot:
  • CAA58449.1()