Prion Protein Antibody, a.a. 109-112, clone 3F4 | EMD Millipore MAB1562 product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

EMD Millipore

other brands :

Oncogene Research Products, Calbiochem, Novagen, Merck, Upstate Biotechnology, Chemicon, LINCO, Novabiochem, Guava

product type :

antibody

product name :

Prion Protein Antibody, a.a. 109-112, clone 3F4

catalog :

MAB1562

quantity :

100 μg

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

3F4

The same clone is also sold as:

Absolute Antibody: Ab00496-1.1, Ab00496-10.7, Ab00496-22.0, Ab00496-10.0, Ab00496-10.6
BioLegend: 800313, 800319, 800302, 800316, 800303, 800310, 800314, 800305, 800306, 800317, 800315, 800301, 800307, 800318, 800304
Novus Biologicals: NBP2-81078-0.2mg

reactivity :

hamsters, human

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, immunohistochemistry - paraffin section

citations: 12

Published Application/Species/Sample/Dilution	Reference
immunocytochemistry; human immunohistochemistry; human western blot; human	Shi Q, Xie W, Zhang B, Chen L, Xu Y, Wang K, et al. Brain microglia were activated in sporadic CJD but almost unchanged in fatal familial insomnia and G114V genetic CJD. Virol J. 2013;10:216 pubmed publisher
immunohistochemistry - paraffin section; hamsters immunocytochemistry; hamsters	Xie W, Shi Q, Zhang J, Zhang B, Gong H, Guo Y, et al. Abnormal activation of microglia accompanied with disrupted CX3CR1/CX3CL1 pathway in the brains of the hamsters infected with scrapie agent 263K. J Mol Neurosci. 2013;51:919-32 pubmed publisher
	Ritchie D, Barria M, Peden A, Yull H, Kirkpatrick J, Adlard P, et al. UK Iatrogenic Creutzfeldt-Jakob disease: investigating human prion transmission across genotypic barriers using human tissue-based and molecular approaches. Acta Neuropathol. 2017;133:579-595 pubmed publisher
	Rouvinski A, Karniely S, Kounin M, Moussa S, Goldberg M, Warburg G, et al. Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs. J Cell Biol. 2014;204:423-41 pubmed publisher
	Xu Y, Zhang J, Tian C, Ren K, Yan Y, Wang K, et al. Overexpression of p62/SQSTM1 promotes the degradations of abnormally accumulated PrP mutants in cytoplasm and relieves the associated cytotoxicities via autophagy-lysosome-dependent way. Med Microbiol Immunol. 2014;203:73-84 pubmed publisher
	Knox K, Carrigan D, Simmons G, Teque F, Zhou Y, Hackett J, et al. No evidence of murine-like gammaretroviruses in CFS patients previously identified as XMRV-infected. Science. 2011;333:94-7 pubmed publisher
	Panigaj M, Brouckova A, Glierova H, Dvorakova E, Simak J, Vostal J, et al. Underestimation of the expression of cellular prion protein on human red blood cells. Transfusion. 2011;51:1012-21 pubmed publisher
	Zomosa Signoret V, Mayoral M, Limon D, Espinosa B, Calvillo M, Zenteno E, et al. Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Sträussler-Scheinker disease. Neuropathology. 2011;31:162-9 pubmed publisher
	Robinson P, Pinheiro T. Phospholipid composition of membranes directs prions down alternative aggregation pathways. Biophys J. 2010;98:1520-8 pubmed publisher
	Diez J, Caballero S, Belda F, Otegui M, Gajardo R, Jorquera J. Elimination capacity of a TSE-model agent in the manufacturing process of Alphanate/Fanhdi, a human factor VIII/VWF complex concentrate. Haemophilia. 2009;15:1249-57 pubmed publisher
	Velasquez Perez L, Rembao Bojorquez D, Guevara J, Guadarrama Torres R, Trejo Contreras A. Creutzfeldt-Jakob disease in Mexico. Neuropathology. 2007;27:419-28 pubmed
	Cooper J, Ladhani K, Minor P. Reference materials for the evaluation of pre-mortem variant Creutzfeldt-Jakob disease diagnostic assays. Vox Sang. 2007;92:302-10 pubmed

product information

Catalog Number :

MAB1562

Subcategory :

Neuroscience

Product Name :

Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4

Product Type :

Antibodies

Clonality :

Monoclonal Antibody

Gene ID :

P04156

Host Name :

Mouse

Antigen :

Prion Protein

Clone :

3F4

Conjugate :

Purified

Isotype :

IgG2a

Product Description :

Anti-Prion Protein Antibody, a.a. 109-112, clone 3F4

Cross Reactivity :

Human;Hamster

Background :

Prions are thought to cause a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and the Creutzfeldt-Jakob disease (CJD) in humans. All thus-far hypothesized prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and thought to be fatal. Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing cell death and tissue damage. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.

ALT Names :

PrP; CD230

Specificity :

Prion protein, amino acid residues 109-112 of human, hamster and feline. Does not react with PrP from any other mammalian species. MAB1562 is reactive to native and denatured forms of PrP. Tissue or cells which have been fixed requires that the epitope be re-exposed (see below). Recognizes both protease sensitive and protease resistant forms of PrP.

Package Size :

100 μg

Uses :

ELISA;Immunohistochemistry;Immunohistochemistry (Paraffin);Immunoprecipitation;Western Blotting

Storage :

Stable for 1 year at -20ºC from date of receipt.