CD59 Antibody - #BF0017
*The optimal dilutions should be determined by the end user.
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# BF0017, RRID:AB_2834066.
16.3A5; 1F5; 1F5 antigen; 20 kDa homologous restriction factor; CD 59; CD_antigen=CD59; CD59; CD59 antigen; CD59 antigen complement regulatory protein; CD59 antigen p18 20; CD59 antigen p18-20 (antigen identified by monoclonal antibodies 16.3A5, EJ16, EJ30, EL32 and G344); CD59 glycoprotein; CD59 molecule; CD59 molecule complement regulatory protein; CD59_HUMAN; Cd59a; Complement regulatory protein; EJ16; EJ30; EL32; FLJ38134; FLJ92039; G344; HRF 20; HRF-20; HRF20; Human leukocyte antigen MIC11; Ly 6 like protein; Lymphocytic antigen CD59/MEM43; MAC inhibitory protein; MAC IP; MAC-inhibitory protein; MAC-IP; MACIF; MACIP; MEM43; MEM43 antigen; Membrane attack complex (MAC) inhibition factor; Membrane attack complex inhibition factor; Membrane inhibitor of reactive lysis; MGC2354; MIC11; MIN1; MIN2; MIN3; MIRL; MSK21; p18 20; Protectin; Surface antigen recognized by monoclonal antibody 16.3A5; T cell activating protein;
Purified recombinant fragment of human CD59 expressed in E. Coli.
PTMs - P13987 As Substrate
Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.
The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.
N- and O-glycosylated. The N-glycosylation mainly consists of a family of biantennary complex-type structures with and without lactosamine extensions and outer arm fucose residues. Also significant amounts of triantennary complexes (22%). Variable sialylation also present in the Asn-43 oligosaccharide. The predominant O-glycans are mono-sialylated forms of the disaccharide, Gal-beta-1,3GalNAc, and their sites of attachment are probably on Thr-76 and Thr-77. The GPI-anchor of soluble urinary CD59 has no inositol-associated phospholipid, but is composed of seven different GPI-anchor variants of one or more monosaccharide units. Major variants contain sialic acid, mannose and glucosamine. Sialic acid linked to an N-acetylhexosamine-galactose arm is present in two variants.
Glycated. Glycation is found in diabetic subjects, but only at minimal levels in nondiabetic subjects. Glycated CD59 lacks MAC-inhibitory function and confers to vascular complications of diabetes.
Cell membrane>Lipid-anchor. Secreted.
Note: Soluble form found in a number of tissues.
Interacts with T-cell surface antigen CD2.
Application: WB Species: Human Sample: MOLM-13 and THP-1 cells
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