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>   home   >   Products   >   Primary Antibodies   >   Signal Transduction   >   Anti-Human CD239 Antibody, clone BRIC221    

Anti-Human CD239 Antibody, clone BRIC221

Mouse Anti-Human Monoclonal Antibody

Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P50895
Reactivity Human
Host Mouse
Clonality Monoclonal
Isotype IgG2b
Clone Names BRIC221
Calculated MW 67405 Da
Additional Information
Other Species Pig
Purification Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Immunogen Human erythrocytes.
Shelf Life 18 months from date of despatch.
Gene ID 4059
Other Names Basal cell adhesion molecule, Auberger B antigen, B-CAM cell surface glycoprotein, F8/G253 antigen, Lutheran antigen, Lutheran blood group glycoprotein, CD239, BCAM, LU, MSK19
Target/Specificity Mouse anti-Human CD239 antibody, clone BRIC221 recognizes human CD239, also known as Lutheran antigen or basal cell aghesion molecule.CD239 is a 597 amino acid, ~85 kDa single pass type I membrane glycoprotein. Clone BRIC221 recognizes a monomorphic determinant expresses on both the 85 and 78 kDa Lutheran (Lu) glycoforms (El Nemer et al.1998). BRIC 221 recognizes an epitope in the fourth extracellular domain of Lu glycoprotein (Parsonset al.1997). Lutheran glycoprotein is a member of the immunoglobulin superfamily and was designated CD239 (B-CAM) at the 7th leucocyte typing workshop. CD239 is expressed by erythrocytes in the peripheral blood.
Preservative & Stabilisers 0.09% Sodium Azide
Storage Store at +4℃ or at -20 ℃.
PrecautionsAnti-Human CD239 Antibody, clone BRIC221 is for research use only and not for use in diagnostic or therapeutic procedures.
Research Areas
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1. Parsons, S.F. et al. (1997) Use of Domain-deletion mutants to locate Lutheran Blood Groups Antigens to each of the five Immunoglobulin Superfamily Domains of the Lutheran Glycoprotein; Elucidation and the Aua/AubPolymorphisms.
Blood 89: 4219-4225. 2. Sakai, E. et al. (2007) Construction of recombinant hemagglutinin derived from the gingipain-encoding gene of Porphyromonas gingivalis, identification of its target protein on erythrocytes, and inhibition of hemagglutination by an interdomain regional peptide.
J Bacteriol. 189: 3977-86. 3. Bruce, L.J. et al. (2003) A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane.
Blood. 101: 4180-8. 4. Kjellgren, D. et al. (2004) Laminin isoforms in human extraocular muscles.
Invest Ophthalmol Vis Sci. 45: 4233-9. 5. Vainionpää, N. et al. (2006) Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells.
Am J Physiol Cell Physiol. 290: C764-75. 6. Chen, J. et al. (2009) Expression of laminin isoforms, receptors, and binding proteins unique to nucleus pulposus cells of immature intervertebral disc.
Connect Tissue Res. 50: 294-306. 7. Määttä, M. et al. (2005) Differential expression of laminin isoforms in ovarian epithelial carcinomas suggesting different origin and providing tools for differential diagnosis.
J Histochem Cytochem. 53: 1293-300. 8. Virtanen, I. et al. (2003) Laminin isoforms in fetal and adult human adrenal cortex.
J Clin Endocrinol Metab. 88: 4960-6. 9. Kikkawa, Y. et al. (2011) An antibody to the lutheran glycoprotein (Lu) recognizing the LU4 blood type variant inhibits cell adhesion to laminin α5.
PLoS One. 6: e23329. 10. Takkunen, M. et al. (2008) Epithelial-mesenchymal transition downregulates laminin alpha5 chain and upregulates laminin alpha4 chain in oral squamous carcinoma cells.
Histochem Cell Biol. 130: 509-25. 11. Hasenson, S. et al. (2005) The immortalized human corneal epithelial cells adhere to laminin-10 by using Lutheran glycoproteins and integrin alpha3beta1.
Exp Eye Res. 81: 415-21. 12. Liu, J.X. et al. (2011) Different impact of ALS on laminin isoforms in human extraocular muscles versus limb muscles.
Invest Ophthalmol Vis Sci. 52: 4842-52. 13. Vuoristo, S. et al. (2009) Laminin isoforms in human embryonic stem cells: synthesis, receptor usage and growth support.
J Cell Mol Med. 13: 2622-33.

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Cat# ABD10137
(40 western blots)
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