|Application ||WB, IHC-F, FC|
|Calculated MW||41400 Da|
|Purification||Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant|
|Shelf Life||18 months from date of despatch.|
|Other Names||Complement decay-accelerating factor, CD55, CD55, CR, DAF|
|Target/Specificity||Mouse anti-Human CD55 antibody, clone 67 recognizes the human CD55 cell surface antigen, a GPI linked molecule also known as decay accelerating factor (DAF). CD55 is expressed by a wide range of cell types. Erythrocyte expression is very weak.CD55 is the complement regulatory protein, decay accelerating factor (DAF) (Lublin and Atkinson 1989). Human CD55 is a ~70kDa glycoprotein (in erythrocytes) anchored in the membrane by glycosylphosphatidylinositol tail. In other cells the apparent molecular weight is somewhat larger. It has a substantial content of O-glycans, and also on N-glycan. DAF binds to activated C4b or C3b complement fragments on the cell surface, preventing the assembly and accelerating the decay of both classical and alternative pathways. DAF carries the Cromer related blood group antigens.DAF has a wide distribution on cells in non-haemopoietic tissues, particularly epithelium and is specifically found at the foetal-maternal interface in placenta (Holmeset al.1990andYanget al.2009). Soluble forms of DAF are found, for example, in plasma, saliva and urine. The antigen on erythrocytes is pronase and chymotrypsin sensitive, but resistant to trypsin.|
|Preservative & Stabilisers||0.09% Sodium Azide|
|Storage||Store at +4℃ or at -20 ℃.|
|Precautions||Anti-Human CD55 Antibody, clone 67 is for research use only and not for use in diagnostic or therapeutic procedures.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
1. Lublin D.M. and Atkinson J.P. (1989) Decay-accelerating factor: biochemistry, molecular biology and function.Ann. Rev. Immunol. 7: 35-58. 2. Daniels G.L. (1989) Cromer-related antigens - blood group determinants on decay-accelerating factor.Vox Sang. 56: 205-211. 3. Holmes C.H. et al. (1990) Preferential expression of the complement regulatory protein decay accelerating factor at the fetomaternal interface during human pregnancy.J. Immunol. 144: 3099-3105. 4. Yang, P. et al. (2009) Expression and modulation of RPE cell membrane complement regulatory proteins.Invest Ophthalmol Vis Sci. 50: 3473-81. 5. van de Sande, M.G. et al. (2011) Different stages of rheumatoid arthritis: features of the synovium in the preclinical phase.Ann Rheum Dis. 70: 772-7. 6. Mo, B. et al. (2006) ECC-1 cells: a well-differentiated steroid-responsive endometrial cell line with characteristics of luminal epithelium.Biol Reprod. 75: 387-94. 7. Araten, D.J. et al. (2005) A quantitative measurement of the human somatic mutation rate.Cancer Res. 65: 8111-7. 8. de Launay, D. et al. (2010) Silencing the expression of Ras family GTPase homologues decreases inflammation and joint destruction in experimental arthritis.Am J Pathol. 177: 3010-24. 9. Gheorghe, K.R. et al. (2011) Prostaglandin E2 synthesizing enzymes in rheumatoid arthritis B cells and the effects of B cell depleting therapy on enzyme expression.PLoS One. ;6: e16378. 10. Kraan, M.C. et al. (2004) T cells, fibroblast-like synoviocytes, and granzyme B+ cytotoxic cells are associated with joint damage in patients with recent onset rheumatoid arthritis.Ann Rheum Dis. 63: 483-8.
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