BCAM Protein (CD239 Protein)

Basal Cell Adhesion Molecule (Cluster of Differentiation 239)

BCAM Products

BCAM Protein, Recombinant

Molecule	Species	Description	Cat. No
BCAM/CD239	Human	BCAM Protein, Recombinant	10238-H02H
BCAM/CD239	Human	BCAM Protein, Recombinant	10238-H08H
BCAM/CD239	Mouse	BCAM Protein, Recombinant	50960-M08H
BCAM/CD239	Mouse	BCAM Protein, Recombinant	50960-M02H

BCAM cDNA Clone

Molecule	Species	Description	Cat. No
BCAM/CD239	Human	Homo sapiens CD239/BCAM transcript variant 1 cDNA Clone(NM_005581.3)	HG10238-M
BCAM/CD239	Mouse	Mouse CD239/BCAM cDNA Clone / ORF Clone	MG50960-G
BCAM/CD239	Human	BCAT2/BCATM cDNA Clone / ORF Clone	HG10228-M
BCAM/CD239	Rat	BCAM cDNA Clone / ORF Clone	RG80222-G

BCAM Related Areas

Cardiovascular>>Red Blood Cell>>BCAM/CD239

Immunology>>Adhesion Molecule>>Cell Adhesion Molecule (IgSF CAM)>>BCAM/CD239

Immunology>>Cluster of Differentiation>>B Cell CD Antigen>>BCAM/CD239

BCAM Alternative Names

CD239, BCAM, AU, LU, MSK19 [Homo sapiens]

Bcam, 1200005K12Rik, B-CAM, Gplu, Lu [Mus musculus]

BCAM Background

The Lutheran (Lu) blood group and basal cell adhesion molecule (BCAM) antigens are both carried by 2 glycoprotein isoforms of the immunoglobulin superfamily representing receptors for the laminin alpha(5) chain. It is a transmembrane receptor with five immunoglobulin-like domains in its extracellular region, and is therefore classified as a member of the immunoglobulin (Ig) gene family. In addition to red blood cells, Lu/BCAM proteins are expressed in endothelial cells of vascular capillaries and in epithelial cells of several tissues. BCAM/LU has a wide tissue distribution with a predominant expression in the basal layer of the epithelium and the endothelium of blood vessel walls. As designated as CD239 recently, BCAM and LU share a significant sequence similarity with the CD146 (MUC18) and CD166, and themselves are adhesion molecules that bind laminin with high affinity. Laminins are found in all basement membranes and are involved in cell differentiation, adhesion, migration, and proliferation. BCAM is upregulated following malignant transformation of some cell types in vivo and in vitro, thus being a candidate molecule involved in tumor progression. In addition, BCAM interacts with integrin in sickle red cells, and thus may potentially play a role in vaso-occlusive episodes.

BCAM Related Studies

1. Kikkawa Y, et al. (2005) Review: Lutheran/B-CAM: a laminin receptor on red blood cells and in various tissues. Connect Tissue Res. 46 (4-5): 193-9.
2. El Nemer W, et al. (2007) Endothelial Lu/BCAM glycoproteins are novel ligands for red blood cell alpha4beta1 integrin: role in adhesion of sickle red blood cells to endothelial cells. Blood. 109 (8): 3544-51.
3. Colin Y, et al. (2008) Red cell and endothelial Lu/BCAM beyond sickle cell disease. Transfus Clin Biol. 15 (6): 402-5.
4. El Nemer W, et al. (2008) Role of Lu/BCAM in abnormal adhesion of sickle red blood cells to vascular endothelium. Transfus Clin Biol. 15 (1-2): 29-33.