Mouse anti Human CD55 antibody, clone BRIC216 recognizes the CD55 antigen, a ~70 kDa glycoprotein also known as Decay Accelerating Factor (DAF). CD55 is distributed on erythrocytes and other circulating blood cells and also on cells in non-haemopoietic tissue particularly epithelium and endothelium. CD55 is also expressed at the foetal-maternal interfaces in placenta.CD55 has reduced expression on individuals with paroxysmal nocturnal haemoglobinuria. Mouse anti Human CD55 antibody, clone BRIC216 has a functional binding affinity to erythrocytes of 8.7 x 107 M-1. The antigen is pronase and trypsin resistant and chymotrypsin sensitive. Mouse anti Human CD55 antibody, clone BRIC216 recognizes the consensus region 3 of the DAF molecule, which contains the functional site, and the antibody blocks the function of DAF.
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
- Buffer Solution
- TRIS buffered saline.
- Preservative Stabilisers
- <0.1% Sodium Azide (NaN3)
- Human fibroblast cell line.
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
- 12 months from date of despatch
- Entrez Gene
- GO Terms
integral to plasma membrane
complement activation, classical pathway
elevation of cytosolic calcium ion concentration
anchored to membrane
innate immune response
- For research purposes only
This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Applications of CD55 antibody
|Functional Assays 1
|Western Blotting 2
- 1 This product contains sodium azide, removal by dialysis is recommended prior to use in functional assays.
- 2Non-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. Suggested working dilutions are given as guide only. 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 © 2021 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Negative Isotype Controls Available
Application Based External Images
Product Specific References
References for CD55 antibody
Coyne, K.E. et al. (1992) Mapping of epitopes, glycosylation sites, and complement regulatory domains in human decay accelerating factor.
J Immunol. 149 (9): 2906-13.
Loberg, R.D. et al. (2006) Inhibition of decay-accelerating factor (CD55) attenuates prostate cancer growth and survival in vivo.
Neoplasia. 8: 69-78.
Triantafilou, M. et al. (2000) A 70 kDa MHC class I associated protein (MAP-70) identified as a receptor molecule for Coxsackievirus A9 cell attachment.
Hum Immunol. 61 (9): 867-78.
Ellison, B.S. et al. (2007) Complement susceptibility in glutamine deprived breast cancer cells.
Cell Div. 2: 20.
Tieng, V. et al. (2002) Binding of Escherichia coli adhesin AfaE to CD55 triggers cell-surface expression of the MHC class I-related molecule MICA.
Proc Natl Acad Sci U S A. 99: 2977-82.
Pahwa, R. et al. (2016) Modulation of PBMC-decay accelerating factor (PBMC-DAF) and cytokines in rheumatoid arthritis.
Mol Cell Biochem. 414 (1-2): 85-94.
Kim, M.S. & Racaniello, V.R. (2007) Enterovirus 70 receptor utilization is controlled by capsid residues that also regulate host range and cytopathogenicity.
J Virol. 81 (16): 8648-55.
Wu, G. et al. (2007) Coagulation cascade activation triggers early failure of pig hearts expressing human complement regulatory genes.
Xenotransplantation. 14 (1): 34-47.
Liszewski, M.K. et al. (2007) Modeling how CD46 deficiency predisposes to atypical hemolytic uremic syndrome.
Mol Immunol. 44: 1559-68.
Wiesner, J. et al. (1997) Host cell factor CD59 restricts complement lysis of Plasmodium falciparum-infected erythrocytes.
Eur J Immunol. 27 (10): 2708-13.
Fodor, W.L. et al. (1995) A novel bifunctional chimeric complement inhibitor that regulates C3 convertase and formation of the membrane attack complex.
J Immunol. 155 (9): 4135-8.
Tu, C.F. et al. (2010) The in vitro protection of human decay accelerating factor and hDAF/heme oxygenase-1 transgenes in porcine aortic endothelial cells against sera of Formosan macaques.
Transplant Proc. 42 (6): 2138-41.
Koch, N. et al. (2009) IL-10 protects monocytes and macrophages from complement-mediated lysis.
J Leukoc Biol. 86 (1): 155-66.
Gullipalli, D. et al. (2018) Antibody Inhibition of Properdin Prevents Complement-Mediated Intravascular and Extravascular Hemolysis.
J Immunol. 201 (3): 1021-9.
Noda, G.S. et al. (2020) Specificities and isotypes of erythrocytes autoantibodies in patients with warm autoimmune hemolytic anemia
Rev Cubana Hematol Inmunol Hemoter 36(4): e1283
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