Overview

  • Product name

    Anti-Prion protein PrP antibody [T16-R]
    See all Prion protein PrP primary antibodies
  • Description

    Rabbit monoclonal [T16-R] to Prion protein PrP
  • Host species

    Rabbit
  • Tested applications

    Suitable for: WB, IPmore details
  • Species reactivity

    Reacts with: Mouse, Rat, Sheep, Cow, Human
  • Immunogen

    Synthetic peptide derived from the N terminal region of Human Prion protein PrP, just before the first octapeptide sequence repeat.

  • Epitope

    Antibody recognizes the epitope located between Thr33 - Gly46
  • Positive control

    • Mouse brain extract; HEK293 cell lysate transfected with Human Prion protein PrP gene; Mouse hippocampus tissue lysate; Recombinant Mouse Prion protein PrP

Properties

  • Form

    Liquid
  • Storage instructions

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.
  • Storage buffer

    pH: 8.00
    Preservative: 0.05% Sodium azide
    Constituents: 0.32% Tris HCl, 1% BSA
  • Concentration information loading...
  • Purity

    Immunogen affinity purified
  • Purification notes

    This immunoglobulin is the product of one single B-cell line from the crude anti-peptide polyclonal anti-serum. This antibody is purified using a proprietary technique and offers a completely post-translationally modified and properly glycosylated antibody. This offers increased stability.
  • Clonality

    Monoclonal
  • Clone number

    T16-R
  • Isotype

    IgG
  • Research areas

Applications

Our Abpromise guarantee covers the use of ab136919 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/1000. Predicted molecular weight: 28 kDa. Incubate the membrane with antibody diluted in blocking buffer 2 hours at room temperature.
IP Use at an assay dependent concentration.

Target

  • Function

    The function of PrP is still under debate. 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 (By similarity). Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G0/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro).
  • Involvement in disease

    Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.
    Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:123400]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.
    Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:600072]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.
    Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:137440]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births.
    Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.
    Defects in PRNP are the cause of kuru (KURU) [MIM:245300]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.
    Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:606688]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.
  • Sequence similarities

    Belongs to the prion family.
  • Domain

    The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing 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.
    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.
  • 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 by SUMO1.
  • Cellular localization

    Cell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.
  • Information by UniProt
  • Database links

  • Alternative names

    • Alternative prion protein; major prion protein antibody
    • AltPrP antibody
    • ASCR antibody
    • CD230 antibody
    • CD230 antigen antibody
    • CJD antibody
    • GSS antibody
    • KURU antibody
    • Major prion protein antibody
    • p27 30 antibody
    • PRIO_HUMAN antibody
    • Prion protein antibody
    • Prion related protein antibody
    • PRIP antibody
    • PRNP antibody
    • PrP antibody
    • PrP27 30 antibody
    • PrP27-30 antibody
    • PrP33-35C antibody
    • PrPC antibody
    • PrPSc antibody
    • Sinc antibody
    see all

Images

  • All lanes : Anti-Prion protein PrP antibody [T16-R] (ab136919) at 1/1000 dilution

    Lane 1 : Mouse brain extract
    Lane 2 : HEK293 cells transfected with Human Prion protein PrP gene
    Lane 3 : HEK293 cells transfected with empty vector

    Lysates/proteins at 200 µg per lane.

    Predicted band size: 28 kDa

  • All lanes : Anti-Prion protein PrP antibody [T16-R] (ab136919) at 1/1000 dilution

    Lane 1 : Prion protein PrP-KO CF10 cell lysate
    Lane 2 : Mouse hippocampus tissue lysate
    Lane 3 : HEK293 cells transfected with
    Mouse Prion protein PrP bearing 3F4 epitope
    Lane 4 : Recombinant Mouse Prion protein PrP

    Lysates/proteins at 30 µg per lane.

    Predicted band size: 28 kDa

References

ab136919 has not yet been referenced specifically in any publications.

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