Human BCAM Protein (His Tag)

AU,CD239,LU,MSK19

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Catalog Number	P10238-H08H
Organism Species	Human
Host	Human Cells
Synonyms	AU,CD239,LU,MSK19
Molecular Weight	The secreted recombinant human BCAM consists of 527 amino acids and predicts a molecular mass of 57.7 KDa. As a result of glycosylation, rh BCAM migrates as approximately 70 KDa band in SDS-PAGE under reducing conditions.
predicted N	Glu 32
SDS-PAGE
Purity	> 98 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the extracellular domain of human BCAM (NP_005572.2) (Met 1-Ala 547) was fused with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area	Cancer |Signal transduction |Cytoskeleton / ECM |Cell Adhesion |Lectin |C-tyep lectin |
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
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.
Reference	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. 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. Colin Y, et al. (2008) Red cell and endothelial Lu/BCAM beyond sickle cell disease. Transfus Clin Biol. 15 (6): 402-5. 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.