ARG56101
anti-CD59 antibody [BRA-10G]
anti-CD59 antibody [BRA-10G] for Functional study,Flow cytometry,ICC/IF and Human
Overview
Product Description | Mouse Monoclonal antibody [BRA-10G] recognizes CD59 |
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Tested Reactivity | Hu |
Tested Application | FACS, FuncSt, ICC/IF |
Host | Mouse |
Clonality | Monoclonal |
Clone | BRA-10G |
Isotype | IgG1, kappa |
Target Name | CD59 |
Antigen Species | Human |
Immunogen | Human K562 tumor cells. |
Conjugation | Un-conjugated |
Alternate Names | EJ30; MIRL; Membrane attack complex inhibition factor; CD antigen CD59; EJ16; Membrane inhibitor of reactive lysis; MIC11; EL32; HRF20; HRF-20; MEM43 antigen; MIN1; MIN2; MIN3; 1F5 antigen; 1F5; MACIF; MAC-IP; MSK21; Protectin; G344; p18-20; CD59 glycoprotein; MEM43; MAC-inhibitory protein; 16.3A5; 20 kDa homologous restriction factor |
Application Instructions
Application Suggestion |
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Application Note | * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. |
Properties
Form | Liquid |
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Purification | Purification with Protein G. |
Buffer | PBS (pH 7.4), 0.05% Sodium azide and 0.1 mg/ml BSA |
Preservative | 0.05% Sodium azide |
Stabilizer | 0.1 mg/ml BSA |
Concentration | 0.2 mg/ml |
Storage Instruction | For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. |
Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
Database Links | |
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Gene Symbol | CD59 |
Gene Full Name | CD59 molecule, complement regulatory protein |
Background | This gene encodes a cell surface glycoprotein that regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. This protein also plays a role in signal transduction pathways in the activation of T cells. Mutations in this gene cause CD59 deficiency, a disease resulting in hemolytic anemia and thrombosis, and which causes cerebral infarction. Multiple alternatively spliced transcript variants, which encode the same protein, have been identified for this gene. [provided by RefSeq, Jul 2008] |
Function | 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. [UniProt] |
Cellular Localization | Cell surface |
Calculated MW | 14 kDa |
PTM | 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. |