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AB134887

Recombinant Human CD59 protein

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(1 Publication)

Recombinant Human CD59 protein is a Human Full Length protein, in the 26 to 102 aa range, expressed in Escherichia coli, with >90%, 5 EU/µg endotoxin level, suitable for SDS-PAGE.

View Alternative Names

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

2 Images
SDS-PAGE - Recombinant Human CD59 protein (AB134887)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human CD59 protein (AB134887)

SDS PAGE analysis of ab134887 (lanes 4-6), using BSA as a reference protein (lanes 1-3).

Lane 1 : 10μg BSA

Lane 2 : 5μg BSA

Lane 3 : 1μg BSA

Lane 4 : 10μl ab134887

Lane 5 : 5μl ab134887

Lane 6 : 1μl ab134887

SDS-PAGE - Recombinant Human CD59 protein (AB134887)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human CD59 protein (AB134887)

SDS PAGE analysis of ab134887 (lanes 4-5), using BSA as a reference protein (lanes 1-3). 4-20% gradient gel was used.

Lane 1 : 10μl BSA

Lane 2 : 5μl BSA

Lane 3 : 1μl BSA

Lane 4 : 20μl ab134887 (Stored at -20°C for 180 days)

Lane 5 : 20μl ab134887 (Stored at -20°C, then shift to 4°C for 30 days)

Key facts

Purity

>90% SDS-PAGE

Endotoxin level

5 EU/µg

Expression system

Escherichia coli

Tags

His tag N-Terminus T7 tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P13987

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MASMTGGQQMGRGHHHHHHGNLYFQGGEFALVQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLEN","proteinLength":"Full Length","predictedMolecularWeight":"12.39 kDa","actualMolecularWeight":null,"aminoAcidEnd":102,"aminoAcidStart":26,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P13987","tags":[{"tag":"His","terminus":"N-Terminus"},{"tag":"T7","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
Biological function summary

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.

Pathways

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.

Specifications

Form

Liquid

Additional notes

ab134887 was refolded using temperature shift inclusion body refolding technology and chromatographically purified.

General info

Function

Potent inhibitor of the complement membrane attack complex (MAC) action, which protects human cells from damage during complement activation (PubMed : 11882685, PubMed : 1698710, PubMed : 2475111, PubMed : 2475570, PubMed : 2606909, PubMed : 9053451). Acts by binding to the beta-haipins of C8 (C8A and C8B) components of the assembling MAC, forming an intermolecular beta-sheet that prevents incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (PubMed : 11882685, PubMed : 1698710, PubMed : 36797260).. The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit complement membrane attack complex (MAC) assembly on cell membranes.

Post-translational modifications

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 (PubMed:10805801). 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 (PubMed:10805801).

Product protocols

Target data

Potent inhibitor of the complement membrane attack complex (MAC) action, which protects human cells from damage during complement activation (PubMed : 11882685, PubMed : 1698710, PubMed : 2475111, PubMed : 2475570, PubMed : 2606909, PubMed : 9053451). Acts by binding to the beta-haipins of C8 (C8A and C8B) components of the assembling MAC, forming an intermolecular beta-sheet that prevents incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (PubMed : 11882685, PubMed : 1698710, PubMed : 36797260).. The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit complement membrane attack complex (MAC) assembly on cell membranes.
See full target information CD59

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

International journal of molecular sciences 24: PubMed37239905

2023

Unveiling CD59-Antibody Interactions to Design Paratope-Mimicking Peptides for Complement Modulation.

Applications

Unspecified application

Species

Unspecified reactive species

Annamaria Sandomenico,Alessia Ruggiero,Emanuela Iaccarino,Angela Oliver,Flavia Squeglia,Miguel Moreira,Luciana Esposito,Menotti Ruvo,Rita Berisio
View all publications

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