Recombinant牛Prion protein PrP (ab753)

概述

描述

  • 性质Recombinant
  • 来源Escherichia coli
  • 氨基酸序列
    • AccessionP10279
    • 种属Cow
    • 序列MKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHV AGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVY YRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQ MCITQYQRESQAYYQRGAS
    • 分子量25 kDa including tags
    • 氨基酸25 to 244
    • 标签His tag C-Terminus

技术指标

Our Abpromise guarantee covers the use of ab753 in the following tested applications.

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

  • 应用

    ELISA

    Western blot

  • 形式Liquid
  • Concentration information loading...

制备和贮存

  • 稳定性和存储

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 10mM Sodium Acetate. pH 4.0

常规信息

  • 别名
    • Alternative prion protein; major prion protein
    • AltPrP
    • ASCR
    • CD230
    • CD230 antigen
    • CJD
    • GSS
    • KURU
    • Major prion protein
    • p27 30
    • PRIO_HUMAN
    • Prion protein
    • Prion related protein
    • PRIP
    • PRNP
    • PrP
    • PrP27 30
    • PrP27-30
    • PrP33-35C
    • PrPC
    • PrPSc
    • Sinc
    see all
  • 功能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).
  • 疾病相关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.
  • 序列相似性Belongs to the prion family.
  • 结构域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.
  • 翻译后修饰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.
  • 细胞定位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

Recombinant Cow Prion protein PrP 图像

  • SDS-PAGE of 2 µg PrPc (lane 1)

Recombinant Cow Prion protein PrP (ab753)参考文献

This product has been referenced in:
  • Legleiter LR  et al. Copper deficiency in the young bovine results in dramatic decreases in brain copper concentration but does not alter brain prion protein biology. J Anim Sci 86:3069-78 (2008). WB . Read more (PubMed: 18599661) »
  • Legleiter LR  et al. Decreased brain copper due to copper deficiency has no effect on bovine prion proteins. Biochem Biophys Res Commun 352:884-8 (2007). Read more (PubMed: 17157816) »

See all 3 Publications for this product

Product Wall

Ab753: is derived from cattle
Ab74200: is derived from sheep ARR genotype
Ab90464: is derived from sheep
Ab90482: is derived from hamster
Ab90483: is derived from hamster
ab140567: is a human prion protein
Thus, it is ab140567 t...

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Thank you for your enquiry.

I can confirm thatto our knowledge Prion protein PrP ab753 is not infectious. It is a recombinant prion protein HIS tagged, not glycosylated and the product will be completely digested by Proteinase K.

...

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Thanks for the additional information. Here is a link to an HRP-conjugated secondary antibody you could for western blotting with ab703: http://www.abcam.com/Rabbit-IgG-secondary-antibody-ab16284.html I hope this is helpful. Please contact me again if ...

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Thank you for your enquiry. I would be happy to help you find a secondary antibody for use with ab703. If you could let me know what application you would use the antibody for and what conjugate you would like attached to the secondary (eg. HRP, biotin...

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Thank you for contacting us. The immunogen used for ab52604 was a smaller peptide from human Prion protein, whereas the protein ab753 is recombinant bovine Prion protein. Ab52604 was not tested for bovine and is not guaranteed to react; a better choice...

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Thank you for your enquiry. Ab753 is a protein solution in 10 mM sodium acetate buffer; it used to come in lyophilized form but now comes reconstituted in 10 mM sodium acetate buffer. Ab1391 is a protein solution in 50 mM sodium acetate buffer. This is...

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Thank you for your enquiry. As described in the data sheet, the buffer is 10 mM sodium acetate buffer pH 4.0. Sorry, we don't produced rb-PrP as lyophilised protein.

The antibody does not require any special handling facilities.

His tag is at the carboxy terminus of the recombinant bovine PrP.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"