Recombinant Human CD59 protein (His tag) is a Human Fragment protein, in the 1 to 101 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
M G I Q G G S V L F G L L L V L A V F C H S G H S L Q C Y N C P N P T A D C K T A V N C S S D F D A C L I T K A G L Q V Y N K C W K F E H C N F N D V T T R L R E N E L T Y Y C C K K D L C N F N E Q L E
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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.
CD59, MIC11, MIN1, MIN2, MIN3, MSK21, CD59 glycoprotein, 1F5 antigen, 20 kDa homologous restriction factor, MAC-inhibitory protein, MEM43 antigen, Membrane attack complex inhibition factor, Membrane inhibitor of reactive lysis, Protectin, HRF-20, HRF20, MAC-IP, MACIF, MIRL
Recombinant Human CD59 protein (His tag) is a Human Fragment protein, in the 1 to 101 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: 100% PBS
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.
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.
CD59 also known as protectin is a protein with a molecular mass of approximately 18-25 kDa. It is widely expressed on the surface of many human cells including red blood cells and various types of leukocytes. CD59 serves as an inhibitor of the complement membrane attack complex (MAC) preventing cell lysis caused by terminal complement proteins. Through this mechanism it regulates complement activation and maintains cell integrity by halting the formation of MAC.
One important feature of CD59 is its role as a glycosylphosphatidylinositol (GPI)-anchored protein involved in safeguarding cells from complement-mediated damage. It does not exist within a larger complex but functions at the cell surface to inhibit the assembly of complement components C5b-9 which form the MAC. This ability to inhibit MAC is essential in maintaining self-tissue from unintended damage during immune responses.
CD59 participates in the regulation of the complement cascade specifically within the terminal pathway. The complement system serves as a bridge between innate and adaptive immunity contributing to processes like opsonization and cell lysis. CD59's inhibitory action directly impacts pathways that utilize terminal components such as C5b. Effective CD59 function prevents excessive complement activation ensuring that an immune response does not damage host tissues. It links closely with other complement regulatory proteins like CD55 which also mitigate complement cascade activation.
Deficiencies or malfunctions in CD59 have notable implications. Paroxysmal nocturnal hemoglobinuria (PNH) is a disorder where lack of CD59 expression on blood cells leads to their increased destruction due to unregulated complement activity. Furthermore CD59's dysfunction or inadequacy also associates with atypical hemolytic uremic syndrome (aHUS) which involves mutant complement regulatory proteins causing overactivation of the complement system. These associations highlight the importance of CD59 in both maintaining cellular health and preventing pathophysiological conditions related to complement overactivity.
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SDS-PAGE analysis of ab276482
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