Anti-Prion protein PrP 抗体 [7B6 / D2] (ab2882)
Key features and details
- Mouse monoclonal [7B6 / D2] to Prion protein PrP
- Suitable for: WB
- Reacts with: Cow, Human
- Isotype: IgG1
製品の概要
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製品名
Anti-Prion protein PrP antibody [7B6 / D2]
Prion protein PrP 一次抗体 製品一覧 -
製品の詳細
Mouse monoclonal [7B6 / D2] to Prion protein PrP -
由来種
Mouse -
特異性
This antibody detects: Human recombinant prion protein. Bovine recombinant, native and PrPres proteinase K treated prion protein. -
アプリケーション
適用あり: WBmore details -
種交差性
交差種: Cow, Human -
免疫原
Recombinant bovine prion protein. Immunization was performed according to the protocol described by Hofmann, J. et al.
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エピトープ
This antibody has been shown to specifically bind between amino acids 123 - 136 and 140 - 160 of bovine prion protein, determined by pepscan (Osman, A.A. et al.). -
特記事項
Reproducibility is key to advancing scientific discovery and accelerating scientists’ next breakthrough.
Abcam is leading the way with our range of recombinant antibodies, knockout-validated antibodies and knockout cell lines, all of which support improved reproducibility.
We are also planning to innovate the way in which we present recommended applications and species on our product datasheets, so that only applications & species that have been tested in our own labs, our suppliers or by selected trusted collaborators are covered by our Abpromise™ guarantee.
In preparation for this, we have started to update the applications & species that this product is Abpromise guaranteed for.
We are also updating the applications & species that this product has been “predicted to work with,” however this information is not covered by our Abpromise guarantee.
Applications & species from publications and Abreviews that have not been tested in our own labs or in those of our suppliers are not covered by the Abpromise guarantee.
Please check that this product meets your needs before purchasing. If you have any questions, special requirements or concerns, please send us an inquiry and/or contact our Support team ahead of purchase. Recommended alternatives for this product can be found below, as well as customer reviews and Q&As.
製品の特性
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製品の状態
Liquid -
保存方法
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. -
バッファー
Preservative: 0.02% Sodium azide -
Concentration information loading...
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精製度
Immunogen affinity purified -
ポリ/モノ
モノクローナル -
クローン名
7B6 / D2 -
アイソタイプ
IgG1 -
軽鎖の種類
kappa -
研究分野
関連製品
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Compatible Secondaries
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Isotype control
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Recombinant Protein
アプリケーション
Our Abpromise guarantee covers the use of ab2882 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
アプリケーション | Abreviews | 特記事項 |
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WB | Use at an assay dependent concentration. Western blot (non-reducing conditions): Use at a concentration of 5 µg/ml. |
ターゲット情報
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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. - Information by UniProt
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参照データベース
- Entrez Gene: 281427 Cow
- Entrez Gene: 5621 Human
- Omim: 176640 Human
- SwissProt: P10279 Cow
- SwissProt: P04156 Human
- Unigene: 472010 Human
- Unigene: 610285 Human
- Unigene: 727471 Human
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別名
- Alternative prion protein; major prion protein antibody
- AltPrP antibody
- ASCR antibody
see all
画像
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ab2882 at a 1
µ g/ml concentration staining ~23 kDa (mature) and ~28 kDa (pro-peptide) native bovine prion protein from brain (M. oblongata; 100µ g comprising 10% homogenised brain, diluted 1:10 in buffer, 10µ l loaded) by Western blot (non-reducing conditions). ab2882 at a 1 µg/ml concentration staining ~23 kDa (mature) and ~28 kDa (pro-peptide) native bovine prion protein from brain (M. oblongata; 100 µg comprising 10% homogenised brain, diluted 1:10 in buffer, 10µl loaded) by Western blot (non-reducing conditions).
データシートおよび資料
参考文献 (1)
ab2882 は 1 報の論文で使用されています。
- Varshney M et al. Prion protein detection using nanomechanical resonator arrays and secondary mass labeling. Anal Chem 80:2141-8 (2008). ELISA . PubMed: 18271602