CD239 antibody | BRIC221
Mouse anti Human CD239 antibody, clone BRIC221 used to look for blocking of Lu-Fc to endogenous α5 laminin in kidney sections.
Image caption:
Lu/B-CAM binding assay on tissue sections.
(A) Binding of Lu-Fc to laminin α5 in adult mouse kidney sections. Sections were incubated with Lu-Fc (upper panel) or Fc (lower panel) at room temperature for 1 hour. Endogenous laminin α5 and bound Lu-Fc were detected with anti-laminin α5 domain LEb/L4b and anti-human IgG, as indicated. Merged pictures showed that laminin α5 and Lu-Fc co-localized at basement membranes. Arrows indicate glomeruli, laminin α5-rich structures. Bar, 100 μm. (B) Binding of Lu-Fc to laminin α5 in adult mouse skeletal muscle sections. Endogenous laminin α2 (upper panel) and α5 (lower panel) were detected with antisera. Bound Lu-Fc was detected with an antibody against human IgG as described above. Lu-Fc only bound to the basement membranes containing α5, primarily neuromuscular junctions. Arrowheads indicate neuromuscular junctions. Bar, 50 μm. (C) Inhibitory effects of anti-Lu/B-CAM antibodies on Lu-Fc binding to laminin α5. After preincubation with anti-Lu/B-CAM antibodies, Lu-Fc was used in the binding assay on tissue sections. Antibody 87207 inhibited the binding of Lu-Fc to endogenous laminin α5.
From: Kikkawa Y, Miwa T, Tohara Y, Hamakubo T, Nomizu M (2011)
An Antibody to the Lutheran Glycoprotein (Lu) Recognizing the LU4 Blood Type Variant Inhibits Cell Adhesion to Laminin α5.
PLoS ONE 6(8): e23329.
Mouse anti Human CD239 antibody, clone BRIC221 epitope mapping by adsorbtion with lutheran deletion and chimeric mutant proteins as measured by ELISA
Image caption:
Identifying the IgSF domains recognized by anti-Lu/B-CAM antibodies.
(A) Diagram of the deletion and chimeric mutant proteins designed to narrow the epitopes of anti-Lu/B-CAM antibodies. For chimeric mutant proteins, the D1 or D1–D2 domains of Lu-Fc were replaced with the analogous domains of melanoma cell adhesion molecule (Mel-CAM). The deletion and chimeric mutant proteins were fused with an IgG Fc domain tag. (B) The mutant proteins purified from conditioned media of HEK293 transfectants were subjected to SDS-PAGE on a 7.5% gel under reducing conditions. Protein was stained with Coomassie Brilliant Blue. Molecular mass standards are indicated. (C) ELISA using the indicated anti-Lu/B-CAM antibodies absorbed with the various recombinant proteins. Wells were coated with 3 μg/ml of Sol-Lu. The mutant proteins were mixed with the diluted antibodies at 1 μg/ml. Each bar represents the mean of triplicate assays. Error bars indicate standard deviation.
From: Kikkawa Y, Miwa T, Tohara Y, Hamakubo T, Nomizu M (2011)
An Antibody to the Lutheran Glycoprotein (Lu) Recognizing the LU4 Blood Type Variant Inhibits Cell Adhesion to Laminin α5.
PLoS ONE 6(8): e23329.
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 (Parsons et 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.
Product Details
- Target Species
- Human
- Species Cross-Reactivity
-
Target Species Cross Reactivity Pig - N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Preparation
- Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
- Buffer Solution
- TRIS buffered glycine
- Preservative Stabilisers
0.09% Sodium Azide - Immunogen
- Human erythrocytes.
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
Storage Information
- Storage
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. - Shelf Life
- 18 months from date of despatch.
More Information
- UniProt
- P50895 Related reagents
- Entrez Gene
- BCAM Related reagents
- GO Terms
- GO:0005055 laminin receptor activity
- GO:0005887 integral to plasma membrane
- GO:0007160 cell-matrix adhesion
- GO:0009897 external side of plasma membrane
- GO:0043236 laminin binding
- Regulatory
- For research purposes only
Applications of CD239 antibody
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| ELISA | |||
| Flow Cytometry | |||
| Immunofluorescence | |||
| Immunohistology - Frozen | |||
| Western Blotting 1 |
- 1Non-reducing conditions required
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.
- Flow Cytometry
- Use 10ul of the suggested working dilution to label 106 cells in 100ul.
Copyright © 2018 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Negative Isotype Controls Available
| Description | Product Code | Pack Size | Applications | List Price | Quantity |
|---|---|---|---|---|---|
| Mouse IgG2b Negative Control | MCA691 | 100 Tests | F |
Product Specific References
References for CD239 antibody
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Parsons, S.F. et al. (1997) Use of domain-deletion mutants to locate Lutheran blood group antigens to each of the five immunoglobulin superfamily domains of the Lutheran glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the Au(a)/Au(b) polymorphisms.
Blood. 89 (11): 4219-25. -
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. -
Bruce, L.J. et al. (2003) A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane.
Blood. 101: 4180-8. -
Kjellgren, D. et al. (2004) Laminin isoforms in human extraocular muscles.
Invest Ophthalmol Vis Sci. 45: 4233-9. -
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. -
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. -
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. -
Virtanen, I. et al. (2003) Laminin isoforms in fetal and adult human adrenal cortex.
J Clin Endocrinol Metab. 88: 4960-6. -
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. -
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. -
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. -
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. -
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. -
Kikkawa, Y. et al. (2016) Down-regulation of cell adhesion via rho-associated protein kinase (ROCK) pathway promotes tumor cell migration on laminin-511
Experimental Cell Research. Apr 8 [Epub ahead of print] -
Vainionpää N et al. (2007) Basement membrane protein distribution in LYVE-1-immunoreactive lymphatic vessels of normal tissues and ovarian carcinomas.
Cell Tissue Res. 328 (2): 317-28. -
Kikkawa Y et al. (2014) Soluble Lutheran/basal cell adhesion molecule is detectable in plasma of hepatocellular carcinoma patients and modulates cellular interaction with laminin-511in vitro.
Exp Cell Res. 328 (1): 197-206. -
Kikkawa, Y. et al. (2008) Laminin alpha 5 mediates ectopic adhesion of hepatocellular carcinoma through integrins and/or Lutheran/basal cell adhesion molecule.
Exp Cell Res. 314 (14): 2579-90. -
Kikkawa, Y. et al. (2007) The LG1-3 tandem of laminin alpha5 harbors the binding sites of Lutheran/basal cell adhesion molecule and alpha3beta1/alpha6beta1 integrins.
J Biol Chem. 282 (20): 14853-60. -
Kikkawa, Y. et al. (2013) The lutheran/basal cell adhesion molecule promotes tumor cell migration by modulating integrin-mediated cell attachment to laminin-511 protein.
J Biol Chem. 288 (43): 30990-1001. -
Enomoto-Okawa, Y. et al. (2017) An Anti-Human Lutheran Glycoprotein Phage Antibody Inhibits Cell Migration on Laminin-511: Epitope Mapping of the Antibody.
PLoS One. 12 (1): e0167860.
