Recombinant Cynomolgus monkey CD46 protein (His tag) (ab271619)
Key features and details
- Expression system: HEK 293 cells
- Purity: >= 80% SDS-PAGE
- Tags: His tag C-Terminus
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Cynomolgus monkey CD46 protein (His tag)
See all CD46 proteins and peptides -
Purity
>= 80 % SDS-PAGE. -
Expression system
HEK 293 cells -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Cynomolgus monkey -
Sequence
MASSGRRERPFSSGRFPGLLLATLVLQLSSFSDACEAPPTFEAMELIGKP KPYYRVGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDEGCYREMCP HIRDPLNGEAILANGSYEFGAELHFICNEGYYLIGKDILYCELKDTVAIW SGKPPLCEKILCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPF SLIGESMIYCGNNSTWSHAAPECKVVKCRFPVVENGKQISGFGKKFYYKA TVMFECDKGYYLNGSDKIVCESNSTWDPPVPKCLKVSTSPTTKSPTSSAS GPRPTYKPPVSNYPGYPKPDEGILNNLDHHHHHHHHHH -
Molecular weight information
This protein runs at a higher MW by SDS-PAGE due to glycosylation. -
Amino acids
35 to 328 -
Tags
His tag C-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab271619 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
pH: 7.40
Constituents: 0.13% Sodium phosphate, 0.64% Sodium chloride, 0.02% Potassium chloride, 20% Glycerol (glycerin, glycerine)
General Info
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Alternative names
- AHUS2
- Antigen defined by monoclonal antibody TRA 2 10
- Antigen identified by monoclonal antibody TRA 2 10
see all -
Function
Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. A number of viral and bacterial pathogens seem to exploit this property and directly induce an immunosuppressive phenotype in T-cells by binding to CD46. -
Tissue specificity
Expressed by all cells except erythrocytes. -
Involvement in disease
Defects in CD46 are a cause of susceptibility to hemolytic uremic syndrome atypical type 2 (AHUS2) [MIM:612922]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. Patients with CD46 mutations seem to have an overall better prognosis compared to patients carrying CFH mutations. -
Sequence similarities
Contains 4 Sushi (CCP/SCR) domains. -
Domain
Sushi domains 1 and 2 are required for interaction with human adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3 is required for Neisseria binding. Sushi domains 3 and 4 are required for interaction with Streptococcus pyogenes M protein and are the most important for interaction with C3b and C4b. -
Post-translational
modificationsN-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding.
Extensively O-glycosylated in the Ser/Thr-rich domain. O-glycosylation is required for Neisseria binding but not for Measles virus or human adenovirus binding.
In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by YES1 in response to infection by Neisseria gonorrhoeae; which promotes infectivity. In T-cells, these isoforms may be phosphorylated by Lck. -
Cellular localization
Cytoplasmic vesicle > secretory vesicle > acrosome inner membrane. Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide. - Information by UniProt
Images
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab271619 has not yet been referenced specifically in any publications.