Lane 1: Human placenta
Lane 2: HUVEC
Lane 3: K562
Recombinant Rabbit monoclonal primary
CD59 Recombinant Rabbit Monoclonal Antibody [JM10-71] (ET1703-28)
NIH-3T3, HUVEC, JAR, K562, Human placenta.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
16.3A5 antibody; 1F5 antibody; 1F5 antigen antibody; 20 kDa homologous restriction factor antibody; CD 59 antibody; CD_antigen=CD59 antibody; CD59 antibody; CD59 antigen antibody; CD59 antigen complement regulatory protein antibody; CD59 antigen p18 20 antibody; CD59 antigen p18-20 (antigen identified by monoclonal antibodies 16.3A5, EJ16, EJ30, EL32 and G344) antibody; CD59 glycoprotein antibody; CD59 molecule antibody; CD59 molecule complement regulatory protein antibody; CD59_HUMAN antibody; Cd59a antibody; Complement regulatory protein antibody; EJ16 antibody; EJ30 antibody; EL32 antibody; FLJ38134 antibody; FLJ92039 antibody; G344 antibody; HRF 20 antibody; HRF-20 antibody; HRF20 antibody; Human leukocyte antigen MIC11 antibody; Ly 6 like protein antibody; Lymphocytic antigen CD59/MEM43 antibody; MAC inhibitory protein antibody; MAC IP antibody; MAC-inhibitory protein antibody; MAC-IP antibody; MACIF antibody; MACIP antibody; MEM43 antibody; MEM43 antigen antibody; Membrane attack complex (MAC) inhibition factor antibody; Membrane attack complex inhibition factor antibody; Membrane inhibitor of reactive lysis antibody; MGC2354 antibody; MIC11 antibody; MIN1 antibody; MIN2 antibody; MIN3 antibody; MIRL antibody; MSK21 antibody; p18 20 antibody; Protectin antibody; Surface antigen recognized by monoclonal antibody; 16.3A5 antibody; T cell activating protein antibody
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. Secreted.
CD59 is a GPI-anchored glycoprotein that is expressed on leukocytes, vascular endothelial cells, various epithelial cells and placenta. CD59 acts together with CD58 in mediating T cell adhesion and activation, and it may be a second ligand of CD2. CD59 functions as a regulator of the terminal pathway of complement by binding to the C8/C9 components of the assembling membrane attack complex (MAC) on host cell membranes, to stop the formation of the lytic pore. CD59 also drives both calcium release and activation of lipid-raft associated signalling molecules such as tyrosine kinases. CD59 gene has two p53-responsive domains that may be implicated in the defense of host cells from damage by the complement system in inflammation, suggesting that p53 could be used to mediate susceptibility of tumor cells to the complement lysis during chemotherapy.