Rabbit polyclonal PRNP antibody (A2583)


Reactivity: Human,Mouse,Rat
Applications: WB,IHC
Conjugation: Unconjugated
Supplier: ABclonal Inc.

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Rabbit polyclonal PRNP antibody (A2583)

Supplier: ABclonal Inc.

Recommended applications: WB,IHC

Recommended dilution:

WB 1:500 – 1:2000 IHC 1:50 – 1:200

Recommended protocols: check protocols

Image descriptions:

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Alternative names:

Check alternative names for the antibody


CJD antibody, GSS antibody, PrP antibody, ASCR antibody, KURU antibody, PRIP antibody, PrPc antibody, CD230 antibody, AltPrP antibody, p27-30 antibody, PrP27-30 antibody, PrP33-35C antibody
Alternative prion protein; major prion protein antibody|PRIP antibody|PRNP antibody|PrP antibody|PrP27 30 antibody|PrP27-30 antibody|PrP33-35C antibody|PrPC antibody|PrPSc antibody|Sinc antibody|Anti-Prion protein PrP antibody [EP1802Y] (ab52604)

SCBT cat No: sc-58581|sc-52969|sc-47729|sc-69896|sc-7693|sc-15312|sc-398451|


Rabbit polyclonal PRNP antibody

Catalogue No.



Human, Mouse, Rat


Recombinant protein of human PRNP





Recommended dilution

WB 1:500 – 1:2000
IHC 1:50 – 1:200







Molecular weight

Predicted: 27kDa/Observed: Refer to Figures


PRNP antibody was tube-contained.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.


PRNP antibody was purified using affinity purification.


Store at -20 Celsius degree. Avoid freeze / thaw cycles.

Alternative antibody names

CJD antibody, GSS antibody, PrP antibody, ASCR antibody, KURU antibody, PRIP antibody, PrPc antibody, CD230 antibody, AltPrP antibody, p27-30 antibody, PrP27-30 antibody, PrP33-35C antibody

Database links

Human UniProt/Swiss-Prot:P04156

Protein names

CJD, GSS, PrP, ASCR, KURU, PRIP, PrPc, CD230, AltPrP, p27-30, PrP27-30, PrP33-35C

Protein function

Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) . Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).

Protein sequence and domain

The normal, monomeric form, PRPN(C), has a mainly alpha-helical structure. Misfolding of this form produces a disease-associated, protease-resistant form, PRPN (Sc), accompanied by a large increase of the beta-sheet content and formation of amyloid fibrils. These fibrils consist of a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. In addition, the heparan-sulfate proteoglycan, GPC1, promotes the association of PRPN (C) to lipid rafts and appears to facilitate the conversion to PRPN (Sc).; Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization.Belongs to the prion family.

Protein post-translational modifications

The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.; Isoform 2 is sumoylated with SUMO1.

Protein cellular localization

Cell membrane; Lipid-anchor, GPI-anchor . Golgi apparatus . Note: Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis.; Isoform 2: Cytoplasm . Nucleus . Note: Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.


The protein encoded by this gene 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. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants.


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Product type

Primary antibody


ABclonal Inc.


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