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Product Info

Source:
Mouse
Application:
ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000, IF/ICC 1:200-1:1000, FCM 1:200-1:400
*The optimal dilutions should be determined by the end user.
*Tips:

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.

Reactivity:
Human
Clonality:
Monoclonal [AFB2044]
Specificity:
CD59 antibody detects endogenous levels of total CD59.
RRID:
AB_2834066
Cite Format: Affinity Biosciences Cat# BF0017, RRID:AB_2834066.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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;

Immunogens

Immunogen:

Purified recombinant fragment of human CD59 expressed in E. Coli.

Uniprot:
Gene(ID):
Description:
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.
Sequence:
MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP

PTMs - P13987 As Substrate

Site PTM Type Enzyme
Y29 Phosphorylation
N43 N-Glycosylation
K63 Acetylation
K66 Acetylation
T76 O-Glycosylation
T77 O-Glycosylation
Y86 Phosphorylation
Y87 Phosphorylation
K90 Ubiquitination
K91 Ubiquitination

Research Backgrounds

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.

PTMs:

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.

Subcellular Location:

Cell membrane>Lipid-anchor. Secreted.
Note: Soluble form found in a number of tissues.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Interacts with T-cell surface antigen CD2.

Research Fields

· Organismal Systems > Immune system > Complement and coagulation cascades.   (View pathway)

· Organismal Systems > Immune system > Hematopoietic cell lineage.   (View pathway)

References

1). The Histone Deacetylase Inhibitor I1 Induces Differentiation of Acute Leukemia Cells With MLL Gene Rearrangements via Epigenetic Modification. Frontiers in Pharmacology (PubMed: 35571127) [IF=5.6]

Application: WB    Species: Human    Sample: MOLM-13 and THP-1 cells

FIGURE 7 The RT-PCR and Western blotting analysis of cell differentiation related genes in MOLM-13 and THP-1 cell lines. (A) The effects of I1 on the mRNA expression of CD59, CD13, HLA-DRA and CIITA evaluated by RT-PCR. MOLM-13 and THP-1 cells were incubated with 1, or 0.7 μM I1 repectively, for 24, 48, or 72 h (B) H3, Ac-H3, H4, Ac-H4, CD59, CD13, HLA-DRA and CIITA protein levels measured by Western blotting analysis. (C) Graph bars show the protein expression visualized and quantified by AI600 imager. MOLM-13 were incubated with 0.25, 0.5, 1 μM I1, or 0.5 μM SAHA for 72 h. THP-1 cells were incubated with 0.175, 0.35, 0.7 μM I1, or 0.7 μM SAHA for 72 h(*p < 0.05, **p < 0.01).

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Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
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