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anti-PRNP antibody :: Prion Protein (PrP) Monoclonal Antibody

Scan QR to view Datasheet Catalog #    MBS312189 anti-PRNP antibody
Unit / Price
0.1 mL  /  $545 +1 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Prion Protein (PrP) (PRNP), Monoclonal Antibody

 Also Known As   

MAb to Prion Protein

 Product Synonym Names    Monoclonal Antibody to Prion Protein (PrP)
 Product Gene Name   

anti-PRNP antibody

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 Chromosome Location    Chromosome: 20; NC_000020.10 (4666797..4682234). Location: 20p13
 OMIM    123400
 3D Structure    ModBase 3D Structure for P04156
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 Clonality    Monoclonal
 Isotype    IgG1, kappa
 Clone Number    7D9
 Host    Host: Mouse
Source: Tissue Culture
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 Specificity    Prion Protein (PrP)
Reacts exceptionally against bovine, sheep, mule deer, elk and mouse PrP. It is 10 fold less reactive to feline, hamster and human PrP. Recognizes both protease sensitive and protease resistant forms of PrP (after denaturing).
 Purity/Purification    IgG fraction, ammonium sulfate precipitated and dialyzed tissue culture supernatant
 Form/Format    Purified, Liquid
 Concentration    1mg/ml (ELISA) (lot specific)
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 Immunogen    Recombinant mouse PrP (amino acids 23-237)
 Affinity Constant    Not determined
 Buffer    PBS
 Preservative    No
 Dry Ice Shipment    Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
 Important Note    Centrifuge before opening to ensure complete recovery of vial contents.
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 Preparation and Storage    The product is best stored undiluted at -20 degree C to -70 degree C. Do not store antibody diluted below 50ug/ml in the absence of protein (i.e.: add 2% BSA).
Shipping: Dry Ice.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of anti-PRNP antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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Product Description specifically for anti-PRNP antibody

   MAb to Prion Protein
Monoclonal Antibody to Prion Protein (PrP)
 Product Categories/Family for anti-PRNP antibody    Monoclonal Antibodies for Neuroscience
 Applications Tested/Suitable for anti-PRNP antibody   

EIA/ELISA, Immunohistochemistry, Western Blot

 Application Notes for anti-PRNP antibody    ELISA (1:20,000-1:50,000)
Western blot (1:10,000-1:25,000)
Immunohistochemistry (1:100-1:500): Epitope must be re-exposed in fixed tissue by pretreatment of tissue using one of the following procedures:
1) Formic acid for 10 minutes at room temperature
2) Hydrolytic autoclaving.
3)HIER (Heat Induced Epitope Retrieval) buffers.
Tissue or cells that have been fixed require epitope retrieval.
Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
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NCBI/Uniprot data below describe general gene information for PRNP. It may not necessarily be applicable to this product.
 NCBI GI #    18490397
 NCBI GeneID    5621
 NCBI Accession #    AAH22532.1 [Other Products]
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 UniProt Primary Accession #    P04156 [Other Products]
 UniProt Secondary Accession #    O60489; P78446; Q15216; Q15221; Q27H91; Q5QPB4; Q8TBG0; Q96E70; Q9UP19 [Other Products]
 UniProt Related Accession #    O75942; P04156; Q16409; Q53YK7; Q540C4; Q5U0K3; Q6FGN5; Q6FGR8; Q6SES1; Q7KYY8 [Other Products]
 Molecular Weight    27,661 Da [Similar Products]
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 NCBI Official Full Name    Prion protein
 NCBI Official Synonym Full Names    prion protein
 NCBI Official Symbol    PRNP [Similar Products]
 NCBI Official Synonym Symbols   
CJD; GSS; PrP; ASCR; PRIP; PrPc; CD230; prion; MGC26679; PrP27-30; PrP33-35C
[Similar Products]
 NCBI Protein Information    major prion protein; p27-30; CD230 antigen; prion protein PrP; OTTHUMP00000030161; OTTHUMP00000030162; OTTHUMP00000030163; OTTHUMP00000161139; prion-related protein; prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
 UniProt Protein Name    Major prion protein
 UniProt Synonym Protein Names   
ASCR; PrP27-30; PrP33-35C
 Protein Family    Major prion protein
 UniProt Gene Name    PRNP [Similar Products]
 UniProt Synonym Gene Names    PRIP; PRP [Similar Products]
 UniProt Entry Name    PRIO_HUMAN
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 NCBI Summary for PRNP    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. Alternative splicing results in multiple transcript variants encoding the same protein. [provided by RefSeq]
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 UniProt Comments for PRNP    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). Ref.21

Subunit structure: Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization. Interacts with GRB2, APP, ERI3/PRNPIP and SYN1. Mislocalized cytosolically exposed PrP interacts with MGRN1; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement

By similarity. Ref.20 Ref.21 Ref.25 Ref.26 Ref.27 Ref.30 Ref.31 Ref.32

Subcellular location: Cell membrane; Lipid-anchor › GPI-anchor. Golgi apparatus

By similarity Ref.17. Isoform 2: Cytoplasm. Nucleus. Note: Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus. Ref.17

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. Ref.20 Ref.21 Ref.25 Ref.26 Ref.30 Ref.32Contains 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. Ref.20 Ref.21 Ref.25 Ref.26 Ref.30 Ref.32

Post-translational modification: The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion. Ref.18Isoform 2 is sumoylated by SUMO1

Polymorphism: The five tandem octapeptide repeats region is highly unstable. Insertions or deletions of octapeptide repeat units are associated to prion disease.

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. Ref.36 Ref.37 Ref.39 Ref.40 Ref.43 Ref.44 Ref.47 Ref.48 Ref.52Defects 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. Ref.36 Ref.37 Ref.39 Ref.40 Ref.43 Ref.44 Ref.47 Ref.48 Ref.52Defects 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. Ref.32 Ref.35Defects 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. Ref.4 Ref.32 Ref.33 Ref.38 Ref.41 Ref.42 Ref.45 Ref.46 Ref.49 Ref.53Defects 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.
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Product References and Citations for anti-PRNP antibody

   • Kascsak, R.J. et al., (2002), "Analysis of parameters influencing the ability to isolate hybridoma clones specific to TSE protein PRP. Conference on transmissible spongiform encephalopathies", Edinburg, Scotland.
• Kascsak, et al.
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 Research Articles on PRNP    1. PrPc prion has a role in mediating synaptic plasticity disruption by soluble amyloid-beta protein.
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Products associated with anti-PRNP antibodyPathways associated with anti-PRNP antibody
 Reference Product  PubMed Publications
 APOE antibody  >35 publications with PRNP and APOE
 CLU antibody  >4 publications with PRNP and CLU
 STIP1 antibody  >1 publications with PRNP and STIP1
 CNTN1 antibody  >1 publications with PRNP and CNTN1
 CLSTN1 antibody  >1 publications with PRNP and CLSTN1
 APLP1 antibody  >1 publications with PRNP and APLP1
 HSPD1 antibody  >1 publications with PRNP and HSPD1
 Products by Pathway  Pathway Diagram
 Axon Guidance Pathway antibodies  Axon Guidance Pathway Diagram
 Glypican 1 Network Pathway antibodies  Glypican 1 Network Pathway Diagram
 NCAM Signaling For Neurite Out-growth Pathway antibodies  NCAM Signaling For Neurite Out-growth Pathway Diagram
 NCAM1 Interactions Pathway antibodies  NCAM1 Interactions Pathway Diagram
 Prion Diseases Pathway antibodies  Prion Diseases Pathway Diagram
 Prion Diseases Pathway antibodies  Prion Diseases Pathway Diagram
Diseases associated with anti-PRNP antibody
 Disease Name  Pubmed Publications
 Prion Diseases Antibodies  >788 publications with PRNP and Prion Diseases
 Neurodegenerative Diseases Antibodies  >564 publications with PRNP and Neurodegenerative Diseases
 Creutzfeldt-Jakob Syndrome Antibodies  >313 publications with PRNP and Creutzfeldt-Jakob Syndrome
 Gerstmann-Straussler-Scheinker Disease Antibodies  >96 publications with PRNP and Gerstmann-Straussler-Scheinker Disease
 Alzheimer Disease Antibodies  >85 publications with PRNP and Alzheimer Disease
 Insomnia, Fatal Familial Antibodies  >76 publications with PRNP and Insomnia, Fatal Familial
 Death Antibodies  >74 publications with PRNP and Death
 Neurologic Manifestations Antibodies  >61 publications with PRNP and Neurologic Manifestations
 Gliosis Antibodies  >37 publications with PRNP and Gliosis
 Neoplasms Antibodies  >26 publications with PRNP and Neoplasms
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