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Mouse Anti-CD59 Recombinant Antibody (p282 H19) (CBMAB-C10517-LY)

The product is antibody recognizes CD59. The antibody p282 H19 immunoassay techniques such as: FC.
See all CD59 antibodies
Published Data
Fig.1 CD59 proteins on the membranes of IBV-infected Vero.
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Summary

Host Animal
Mouse
Specificity
Human, Chimpanzee, Baboon, Monkey
Clone
p282 H19
Antibody Isotype
IgG2a, κ
Application
FC

Basic Information

Specificity
Human, Chimpanzee, Baboon, Monkey
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Preservative
0.09% sodium azide
Concentration
0.5 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
CD59 Molecule (CD59 Blood Group)
Introduction
CD59 (CD59 Molecule (CD59 Blood Group)) is a Protein Coding gene. Diseases associated with CD59 include Hemolytic Anemia, Cd59-Mediated, With Or Without Immune-Mediated Polyneuropathy and Hemolytic Anemia. Among its related pathways are Creation of C4 and C2 activators and Transport to the Golgi and subsequent modification. Gene Ontology (GO) annotations related to this gene include complement binding.
Entrez Gene ID
Human966
Chimpanzee739046
Monkey693402
Baboon101016369
UniProt ID
HumanP13987
ChimpanzeeG2HDS7
MonkeyQ8SQ46
BaboonQ28785
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.
Biological Process
Blood coagulation Source: ProtInc
Cell surface receptor signaling pathway Source: ProtInc
COPII vesicle coating Source: Reactome
Endoplasmic reticulum to Golgi vesicle-mediated transport Source: Reactome
Negative regulation of activation of membrane attack complex Source: GO_Central
Neutrophil degranulation Source: Reactome
Regulation of complement activation Source: MGI
Regulation of complement-dependent cytotoxicity Source: MGI
Cellular Location
Secreted; Cell membrane. Soluble form found in a number of tissues.
Involvement in disease
Hemolytic anemia, CD59-mediated, with or without polyneuropathy (HACD59): An autosomal recessive disorder characterized by infantile onset of chronic hemolysis and a relapsing-remitting polyneuropathy, often exacerbated by infection, and manifested as hypotonia, limb muscle weakness, and hyporeflexia.
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.

Kawaguchi, K., Yamamoto-Hino, M., & Goto, S. (2021). SPPL3-dependent downregulation of the synthesis of (neo) lacto-series glycosphingolipid is required for the staining of cell surface CD59. Biochemical and Biophysical Research Communications, 571, 81-87.

Jia, Y., Qi, Y., Wang, Y., Ma, X., Xu, Y., Wang, J., ... & Han, S. (2019). Overexpression of CD59 inhibits apoptosis of T-acute lymphoblastic leukemia via AKT/Notch1 signaling pathway. Cancer cell international, 19(1), 1-14.

Yu, J., Murthy, V., & Liu, S. L. (2019). Relating GPI-anchored Ly6 proteins uPAR and CD59 to viral infection. Viruses, 11(11), 1060.

Ueda, M., Sato, Y., Horie, A., Tani, H., Miyazaki, Y., Okunomiya, A., ... & Mandai, M. (2019). Endovascular trophoblast expresses CD59 to evade complement-dependent cytotoxicity. Molecular and cellular endocrinology, 490, 57-67.

Karbian, N., Eshed-Eisenbach, Y., Tabib, A., Hoizman, H., Morgan, B. P., Schueler-Furman, O., ... & Mevorach, D. (2018). Molecular pathogenesis of human CD59 deficiency. Neurology Genetics, 4(6).

Wang, L. N., Gao, M. H., Wang, B., Cong, B. B., & Zhang, S. C. (2018). A role for GPI-CD59 in promoting T-cell signal transduction via LAT. Oncology letters, 15(4), 4873-4881.

Fülöp, G., Brameshuber, M., Arnold, A. M., Schütz, G. J., & Sevcsik, E. (2018). Determination of the membrane environment of CD59 in living cells. Biomolecules, 8(2), 28.

Zhang, R., Liu, Q., Liao, Q., & Zhao, Y. (2018). CD59: a promising target for tumor immunotherapy. Future Oncology, 14(8), 781-791.

Panda, S., Kumari, L., & Panda, S. (2018). Structural analysis of CD59 of chinese tree shrew: A New reference molecule for human immune system specific CD59 drug discovery. Current drug discovery technologies, 15(4), 326-334.

Salviano-Silva, A., Petzl-Erler, M. L., & Boldt, A. B. W. (2017). CD59 polymorphisms are associated with gene expression and different sexual susceptibility to pemphigus foliaceus. Autoimmunity, 50(6), 377-385.

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For research use only. Not intended for any clinical use.

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