Tailor-made Antibodies
and Tools for Life Science
Home|||||Technical Support

Oligo-Abeta-pE3 antibody - 218 511

Oligo-Abeta-pE3 is a major component of neuritic plaques in Alzheimer's disease
Mouse monoclonal purified IgG
Cat. No.: 218 511
Amount: 100 µg
Price: $415.00
Cat. No. 218 511 100 µg purified IgG, lyophilized. Albumin and azide were added for stabilization. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 500 (see remarks) gallery  
IP: not tested yet
ICC: not tested yet
IHC: 1 : 100 gallery  
IHC-P: 1 : 100 (see remarks) gallery  
ELISA: yes (see remarks)
Important note for users The mouse monoclonal antibody clone 9D5, Cat. No. 218 511, is patented (patent application PCT/EP2011/002739). By purchasing this antibody the customer acquires rights to use this product for research purposes only. Any diagnostic and therapeutic in vitro or in vivo use is explicitly excluded.
Clone 9D5
Subtype IgG2b (κ light chain)
Immunogen Synthetic peptide corresponding to AA 3 to 38 from human Oligo-Abeta-pE3 (UniProt Id: P05067)
Reactivity Reacts with: human (P05067), mouse (P12023).
Other species not tested yet.
Specificity Recognizes specific oligomeric structures formed preferentially by Abeta-pE3.
Remarks

WB: We recommend the Invitrogen NativePAGE system in combination with PVDF blotting membranes. Boil membrane after blotting for 3min.
Peptide preparation: Synthetic Abeta peptides were monomerized in 70 % formic acid, and the solvent was evaporated in a speed-vac immediately. Prior to each experiment, peptides were dissolved in 0.3 % ammonia, underwent ultrasonic treatment, and were further diluted to an end concentration of 0.15 % ammonia.
IHC-P: Antigen retrieval with formic acid is required.
ELISA: Suitable as capture antibody for sandwich-ELISA with cat. no. 218 011BT as detector antibody.

Data sheet 218_511.pdf

References for Oligo-Abeta-pE3 - 218 511

Identification of low molecular weight pyroglutamate A{beta} oligomers in Alzheimer disease: a novel tool for therapy and diagnosis.
Wirths O, Erck C, Martens H, Harmeier A, Geumann C, Jawhar S, Kumar S, Multhaup G, Walter J, Ingelsson M, Degerman-Gunnarsson M, et al.
The Journal of biological chemistry (2010) 28553: 41517-24. 218 511 WB, IHC, ELISA
I716F AβPP mutation associates with the deposition of oligomeric pyroglutamate amyloid-β and α-synucleinopathy with Lewy bodies.
Sieczkowski E, Milenkovic I, Venkataramani V, Giera R, Ströbel T, Höftberger R, Liberski PP, Auff E, Wirths O, Bayer TA, Kovacs GG, et al.
Journal of Alzheimer's disease : JAD (2015) 441: 103-14. 218 511 IHC; tested species: human
Oxidative Stress during the Progression of β-Amyloid Pathology in the Neocortex of the Tg2576 Mouse Model of Alzheimer's Disease.
Porcellotti S, Fanelli F, Fracassi A, Sepe S, Cecconi F, Bernardi C, Cimini A, Cerù MP, Moreno S
Oxidative medicine and cellular longevity (2015) 2015: 967203. 218 511 IHC
Oligomeric pyroglutamate amyloid-β is present in microglia and a subfraction of vessels in patients with Alzheimer's disease: implications for immunotherapy.
Wirths O, Hillmann A, Pradier L, Härtig W, Bayer TA
Journal of Alzheimer's disease : JAD (2013) 354: 741-9. 218 511 IHC
Antibody 9D5 recognizes oligomeric pyroglutamate amyloid-β in a fraction of amyloid-β deposits in Alzheimer's disease without cross-reactivity with other protein aggregates.
Venkataramani V, Wirths O, Budka H, Härtig W, Kovacs GG, Bayer TA
Journal of Alzheimer's disease : JAD (2012) 292: 361-71. 218 511 IHC
Identification of low molecular weight pyroglutamate A{beta} oligomers in Alzheimer disease: a novel tool for therapy and diagnosis.
Wirths O, Erck C, Martens H, Harmeier A, Geumann C, Jawhar S, Kumar S, Multhaup G, Walter J, Ingelsson M, Degerman-Gunnarsson M, et al.
The Journal of biological chemistry (2010) 28553: 41517-24. 218 511 WB, IHC, ELISA
Focusing the amyloid cascade hypothesis on N-truncated Abeta peptides as drug targets against Alzheimer's disease.
Bayer TA, Wirths O
Acta neuropathologica (2014) 1276: 787-801. 218 511 IHC-P; tested species: human
Identification of low molecular weight pyroglutamate A{beta} oligomers in Alzheimer disease: a novel tool for therapy and diagnosis.
Wirths O, Erck C, Martens H, Harmeier A, Geumann C, Jawhar S, Kumar S, Multhaup G, Walter J, Ingelsson M, Degerman-Gunnarsson M, et al.
The Journal of biological chemistry (2010) 28553: 41517-24. 218 511 WB, IHC, ELISA
Intraneuronal Aβ as a trigger for neuron loss: can this be translated into human pathology?
Bayer TA, Wirths O
Biochemical Society transactions (2011) 394: 857-61. 218 511
Cat. No.: 218 511
Amount: 100 µg
Price: $415.00
Identification of low molecular weight pyroglutamate A{beta} oligomers in Alzheimer disease: a novel tool for therapy and diagnosis.
Wirths O, Erck C, Martens H, Harmeier A, Geumann C, Jawhar S, Kumar S, Multhaup G, Walter J, Ingelsson M, Degerman-Gunnarsson M, et al.
The Journal of biological chemistry (2010) 28553: 41517-24. 218 511 WB, IHC, ELISA
I716F AβPP mutation associates with the deposition of oligomeric pyroglutamate amyloid-β and α-synucleinopathy with Lewy bodies.
Sieczkowski E, Milenkovic I, Venkataramani V, Giera R, Ströbel T, Höftberger R, Liberski PP, Auff E, Wirths O, Bayer TA, Kovacs GG, et al.
Journal of Alzheimer's disease : JAD (2015) 441: 103-14. 218 511 IHC; tested species: human
Oxidative Stress during the Progression of β-Amyloid Pathology in the Neocortex of the Tg2576 Mouse Model of Alzheimer's Disease.
Porcellotti S, Fanelli F, Fracassi A, Sepe S, Cecconi F, Bernardi C, Cimini A, Cerù MP, Moreno S
Oxidative medicine and cellular longevity (2015) 2015: 967203. 218 511 IHC
Oligomeric pyroglutamate amyloid-β is present in microglia and a subfraction of vessels in patients with Alzheimer's disease: implications for immunotherapy.
Wirths O, Hillmann A, Pradier L, Härtig W, Bayer TA
Journal of Alzheimer's disease : JAD (2013) 354: 741-9. 218 511 IHC
Antibody 9D5 recognizes oligomeric pyroglutamate amyloid-β in a fraction of amyloid-β deposits in Alzheimer's disease without cross-reactivity with other protein aggregates.
Venkataramani V, Wirths O, Budka H, Härtig W, Kovacs GG, Bayer TA
Journal of Alzheimer's disease : JAD (2012) 292: 361-71. 218 511 IHC
Identification of low molecular weight pyroglutamate A{beta} oligomers in Alzheimer disease: a novel tool for therapy and diagnosis.
Wirths O, Erck C, Martens H, Harmeier A, Geumann C, Jawhar S, Kumar S, Multhaup G, Walter J, Ingelsson M, Degerman-Gunnarsson M, et al.
The Journal of biological chemistry (2010) 28553: 41517-24. 218 511 WB, IHC, ELISA
Focusing the amyloid cascade hypothesis on N-truncated Abeta peptides as drug targets against Alzheimer's disease.
Bayer TA, Wirths O
Acta neuropathologica (2014) 1276: 787-801. 218 511 IHC-P; tested species: human
Identification of low molecular weight pyroglutamate A{beta} oligomers in Alzheimer disease: a novel tool for therapy and diagnosis.
Wirths O, Erck C, Martens H, Harmeier A, Geumann C, Jawhar S, Kumar S, Multhaup G, Walter J, Ingelsson M, Degerman-Gunnarsson M, et al.
The Journal of biological chemistry (2010) 28553: 41517-24. 218 511 WB, IHC, ELISA
Intraneuronal Aβ as a trigger for neuron loss: can this be translated into human pathology?
Bayer TA, Wirths O
Biochemical Society transactions (2011) 394: 857-61. 218 511
Background

Amyloid deposits, also called plaques, of Alzheimer's patients consist of several protein components like the amyloid beta-peptides (Abeta, ) 1-40/42 and additional C- and N-terminally truncated and modified fragments. Very abundant are the isoaspartate (isoAsp)-Abeta and pyroglutamyl (pGlu)-Abeta peptides. The latter are formed by cyclization of the N-terminal glutamate at position 3 or 11 catalyzed by glutaminyl cyclase (QC) resulting in very amyloidogenic and neurotxic variants of Abeta; Abeta-pE3 and Abeta pE11.
In contrast to extracellular plaques that do not perfectly correlate with Alzheimer´s disease intraneuronal Abeta accumulation and vascular Abeta deposits have gained more and more evidence to be among the crucial factors responsible for progressive neuron loss.