Anti-Prion protein antibody, mouse monoclonal (7A1)

Product#: 65-903
$288.00
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Anti-Prion protein antibody, mouse monoclonal (7A1) 
 

DiagnoCine offers excellent  PRNP I CD230 I Prion Protein Antibodies  to researchers studying Neurodegeneration, Neuritogenesis, Neuronal Homeostasis, Proteopathies, Cell Signalling, Cell Adhesion, Plasma, and Stress. 

Human diseases include Creutzfeldt-Jakob Disease, Gerstmann-Straussler Disease, Kuru, Huntington Disease, Fatal Familial Insomnia (FFI), Sporadic Human Prion Disease, and Dementia. 
 
Anti-Prion protein | PRNP | CD230 Antibodies has excellent quality and this highly pure antibody can be adapted for Western Blots, ELISA, Immunohistochemistry, Immunoprecipitation research with optimization.


General information 

Cat. No. 65-903 
Size 50 ug
Host Species Mouse 
label :Unlabeled 
Clone :7A1 
Immunogen Recombinant human PrP lacking GPI anchor expressed and purified from rabbit kidney cell line RK13.
Reactivity Reacts with human Prion but not with mouse Prion. Other species have not been tested.

Antibody 

Mouse monoclonal antibody, IgG1 kappa. The hybridoma was established in the laboratory of
    Prof. N. Kitamoto at University of Hyogo.
Form  :Purified IgG 1 mg/ml in PBS(-), 50% glycerol, filtersterilized (azide-free)
Application :1. Western blotting (~0.5 μg/ml)
:2. ELISA
:3. 
Other applications have not been tested.
Storage Sent at 4℃ or at -20℃ and upon arrival, centrifuge briefly, and store at -20℃
Data Link 

:UniProtKB/Swiss-Prot P04156


Description 

Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neuron and glia cells as well as immune and reproductive cells. Mutations in the octapeptide repeat regions as well as elsewhere in this gene have been associated with neurodegenerative diseases such as Creutzfeldt Jakob disease, fatal familial insomnia, Gerstmann Straussler disease, Huntington disease like 1, and kuru. The infectious isoform of PrPC, known as PrPSc, is able to convert normal PrPP C proteins into the infectious isoform, which is insoluble amyloid aggregate, by changing their conformation (1). 

Mature PrP protein in human consists of 209 amino acids. Several topological forms exist; one cell surface form anchored via glycolipid and two transmembrane forms, which are responsible for appearance of multiple bands in SDS-PAGE (Figure).

 

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Figure Identification of Prion protein in crude cell extract by Western blotting using
the monoclonal antibody 2C5-5.

Lane 1 Extract of rabbit kidney cells RK13 over-expressing Prion protein
Lane 2 Negative control; extract of the vector infected cells
Lane 3 Negative control; extract of RK13 cells


References

  1. Sakudo A et al ”GPI-anchorless human prion protein is secreted and glycosylated but lacks superoxide dismutase activity” Int J Mol Med 21: 217-222 (2008) PMID: 18204788

*This antibody has been used in Ref.

 

Aliases for PRNP Gene

  • Prion Protein 2 3 5
  • AltPrP 2 3 4
  • Alternative Prion Protein 3 4
  • Major Prion Protein 3 4
  • CD230 Antigen 3 4
  • PrP33-35C 3 4
  • PrP27-30 3 4
  • P27-30 2 3
  • CD230 2 3
  • ASCR 3 4
  • PRIP 3 4
  • PrP 3 4
  • PRP 2 4
  • Gerstmann-Strausler-Scheinker Syndrome 2
  • Creutzfeldt-Jakob Disease 2
  • Fatal Familial Insomnia 2
  • Prion Protein (P27-30) 2
  • Prion-Related Protein 3
  • ALTPRP 4
  • KURU 3
  • PrPc 3
  • PRNP 5
  • CJD 3
  • GSS 3

 
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