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
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
Tested Application Dilution
FACS0.5 - 1 µg/10^6 cells in 0.1ml
FuncStAssay-dependent
ICC/IF0.5 - 1 µg/ml
Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.

Properties

Form Liquid
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

GeneID: 966 Human CD59

Swiss-port # P13987 Human CD59 glycoprotein

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.