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PRNP antibody (Prion Protein) (AA 93-109)

Details for Product anti-PRNP Antibody No. ABIN264042, Supplier: Log in to see
Antigen
  • AA960666
  • AI325101
  • AltPrP
  • ASCR
  • BIMP2
  • CARMA2
  • CD230
  • CJD
  • cjd
  • GSS
  • KURU
  • MGC84114
  • p27-30
  • prion
  • PRIP
  • Prn
  • Prn-i
  • Prn-p
  • PRNP
  • prp
  • Prp
  • PrP
  • PRP
  • prp(c)
  • prP27-30
  • PrP27-30
  • PrP33-35C
  • prP33-35C
  • PrP
  • PRPC
  • PrPc
  • PrPC
  • PrPSc
  • PSORS2
  • PSS1
  • Sinc
  • SIP
Epitope
AA 93-109
14
13
12
10
8
8
7
4
2
2
2
2
2
2
2
1
1
1
1
1
1
Reactivity
Cow (Bovine), Hamster, Human, Mouse (Murine), Sheep (Ovine)
117
63
50
44
42
5
4
2
2
2
1
1
1
1
1
1
1
1
1
1
1
Host
Mouse
97
69
27
1
Clonality (Clone)
Monoclonal ()
Conjugate
This PRNP antibody is un-conjugated
9
7
6
4
3
3
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
Application
Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
130
98
51
46
22
11
8
8
5
5
3
2
2
Supplier
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Immunogen Full-length recombinant PrP
Clone 6D11
Isotype IgG2a
Specificity This antibody reacts with both the PrPc and PrPsc forms.
Characteristics Synonyms: Major prion protein, PrP27-30, PrP33-35C, ASCR, PRNP, PRIP
Purification Protein A Chromatography
Alternative Name CD230 / PrP (PRNP Antibody Abstract)
Background Prion protein PrP is a membrane glycosylphosphatidylinositol anchored glycoprotein that tends to aggregate into rod like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt Jakob disease, fatal familial insomnia, Gerstmann Straussler disease, Huntington disease like 1, and kuru. Two transcript variants encoding the same protein have been found for this gene. All prion diseases share the same molecular pathogenic mechanism that involves conversion of normal cellular prion protein (PrPc) into a form that is insoluble in non ionic detergent and partially resistant to proteases (PrPsc). Both PrPsc and PrPc are encoded within a single exon of a chromosomal gene as a protein of ~ 250 amino acids. Many mammalian PrPs have a 22 amino acid N terminal signal sequence and 23 amino acid C terminal signal sequence encoding for attachment of a glycosylphosphatidylinositol anchor. The mature protein of 209 amino acids contains one disulfide bond and has two sites of asparagine linked glycosylation.Synonyms: ASCR, Major prion protein, PRIP, PRNP, PrP27-30, PrP33-35C
Gene ID 5621
UniProt P04156
Research Area CD Antigens, Surface Receptors of Immune Cells
Application Notes ELISA. Western blot. Immunohistochemistry: Epitope must be re-exposed in fixed tissues by pretreatment usingone of the following procedures: 1.70 % Formic acid for 10-30 minutes at room temperature.2. Hydrolytic autoclaving
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 2.0 mg/mL
Buffer PBS without preservatives
Preservative Without preservative
Storage -20 °C
Storage Comment Store the antibody at -20 °C. Avoid repeated freezing and thawing. Do not store antibody diluted below 50?g/ml in the absence of protein (i. e. add 2% BSA).
Shelf life: one year from despatch.
Expiry Date 12 months
Background publications Sigurdsson, Sy, Li, Scholtzova, Kascsak, Kascsak, Carp, Meeker, Frangione, Wisniewski: "Anti-prion antibodies for prophylaxis following prion exposure in mice." in: Neuroscience letters, Vol. 336, Issue 3, pp. 185-7, 2002

Kascsak, Fersko, Pulgiano, Rubenstein, Carp: "Immunodiagnosis of prion disease." in: Immunological investigations, Vol. 26, Issue 1-2, pp. 259-68, 1997

Kascsak, Tonna-DeMasi, Fersko, Rubenstein, Carp, Powers: "The role of antibodies to PrP in the diagnosis of transmissible spongiform encephalopathies." in: Developments in biological standardization, Vol. 80, pp. 141-51, 1994

Kascsak, Rubenstein, Merz, Tonna-DeMasi, Fersko, Carp, Wisniewski, Diringer: "Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins." in: Journal of virology, Vol. 61, Issue 12, pp. 3688-93, 1987