Anti-Prion protein PrP 抗体 [EP1802Y] (ab52604)

製品の概要

• 製品名Anti-Prion protein PrP antibody [EP1802Y]
  Prion protein PrP 一次抗体 製品一覧
• 製品の詳細
  Rabbit monoclonal [EP1802Y] to Prion protein PrP
• アプリケーション適用あり: WB, Flow Cyt, IHC-P, ICC/IFmore details
  適用なし: IP
• 種交差性
  交差種: Mouse, Rat, Human
  
• 免疫原

  A synthetic peptide corresponding to residues near the C-terminus of human Prion protein PrP.

• ポジティブ･コントロール
  • Fetal brain lysate; brain glioma tissue.
• 特記事項

  Produced using Abcam's RabMAb^® technology. RabMAb^® technology is covered by the following U.S. Patents, No. 5, 675, 063 and/or 7, 429, 487.

  This product is a recombinant rabbit monoclonal antibody.

製品の特性

• 製品の状態Liquid
• 保存方法Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
• バッファーPBS 49%,Sodium azide 0.01%,Glycerol 50%,BSA 0.05%
• 精製度Tissue culture supernatant
• ポリ/モノモノクローナル
• クローン名EP1802Y
• アイソタイプIgG
• 研究分野
  • Neuroscience
  • Neurology process
  • Neurodegenerative disease
  • Prions

  • Stem Cells
  • Hematopoietic Progenitors
  • Surface Molecules

関連製品

• Compatible Secondaries
  • Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (ab150077)
  • Goat Anti-Rabbit IgG H&L (HRP) (ab205718)
• Related Products
  • Goat Anti-Rabbit IgG H&L (DyLight® 488) preadsorbed (ab96899)

アプリケーション

ターゲット情報

• 機能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).
• 関連疾患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.
• 配列類似性Belongs to the prion family.
• ドメイン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.
• 翻訳後修飾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.
• 細胞内局在Cell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.

• Target information above from: UniProt accession P04156 The UniProt Consortium
  The Universal Protein Resource (UniProt) in 2010
  Nucleic Acids Res. 38:D142-D148 (2010) .

  Information by UniProt
• 参照データベース
  • Entrez Gene: 5621 Human
  • Entrez Gene: 19122 Mouse
  • Entrez Gene: 24686 Rat
  • Omim: 176640 Human
  • SwissProt: P04156 Human
  • SwissProt: P04925 Mouse
  • SwissProt: P13852 Rat
  • Unigene: 472010 Human

  • Unigene: 610285 Human
  • Unigene: 727471 Human
  • Unigene: 648 Mouse
  • Unigene: 3936 Rat

  see all
• 別名
  • 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