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Abeta40 antibody - 218 202

Abeta peptides are major components of neuritic plaques in Alzheimer's disease
Rabbit polyclonal antiserum
Cat. No.: 218 202
Amount: 200 µl
Price: $355.00
Cat. No. 218 202 200 µl antiserum, lyophilized. For reconstitution add 200 µl H2O, then aliquot and store at -20°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
WB: 1 : 1000 (see remarks) gallery  
IP: not tested yet
ICC: not tested yet
IHC: not tested yet (see remarks)
IHC-P: 1 : 100 up to 1 : 500 (see remarks) gallery  
ELISA: (see remarks)
Immunogen Synthetic peptide corresponding to AA 33 to 40 from human Abeta40 (UniProt Id: P05067)
Reactivity Reacts with: human (P05067), rat (P08592), mouse (P12023).
Other species not tested yet.
Specificity Specific for Abeta 40, no cross reactivity to Abeta 38 and 42.

WB: Detects purified Abeta 40. Complex samples like brain extracts still have to be tested. Boil membrane after blotting for 3min.
IHC: Antigen retrieval with formic acid is required.
IHC-P: Antigen retrieval with formic acid is required.
ELISA: suitable as capture and detector antibody for sandwich-ELISA.

Data sheet 218_202.pdf
Cat. No.: 218 202
Amount: 200 µl
Price: $355.00

Amyloid deposits, also called plaques, of Alzheimer's patients consist of several protein components like the amyloid beta-peptides (Abeta, Aβ) 1-40/42/43 and additional C- and N-terminally modified fragments of Abeta as for instance Abeta pE3 and Abeta pE11.
An additional Abeta variant, Abeta 38, is more soluble compared to other Abeta species and is not found in plaques of sporadic Alzheimer´s cases. However, it is detected in the blood-vessel walls of a subset of patients with severe cerebral amyloid angiopathy. It especially accumulates in brains of patients carrying mutations in the Abeta coding region.
Cleavage of amyloid precursor protein APP by β- and γ- secretases results in the generation of the Aβ (βA4)peptide, whereas α-secretase cleaves within the Aβ sequence and prevents the formation of Abeta from APP.