Amyloid beta (free N-term, APP reactive) Mouse Monoclonal Antibody [Clone ID: 19H5]

SKU AM00006PU-N

Amyloid beta (free N-term, APP reactive) mouse monoclonal antibody, clone 19H5, Purified

Product Data

• Clone Name: 19H5
• Application: ELISA, WB
• Recommended Dilution: ELISA: 0.05 µg/ml.; Western blot: 1 µg/ml for HRPO/ECL detection. ; Recommended blocking buffer: Casein/Tween 20 based blocking and blot incubation buffer.
• Reactivity: Human
• Antibody Host: Mouse
• Isotype: IgG1
• Clonality: Monoclonal
• Immunogen: N-terminal peptide conjugated to KLH.
• Specificity: This antibody recognizes the free N-Terminus of the βA4 polypeptide. ; The antibody crossreacts with APP.
• Buffer: 1 ml 2 x PBS containing PEG and Sucrose; State: Purified; State: Lyophilized purified IgG fraction; Preservative: 0.09% Sodium Azide
• Reconstitution Method: Restore with 1 ml H₂O (15 min, RT).
• Purification: Subsequent Thiophilic Adsorption and Size Exclusion Chromatography
• Conjugation: Unconjugated
• Storage: Prior to reconstitution store at -20°C. ; Following reconstitution store the antibody undiluted at 2-8°C for one month ; or (in aliquots) at -80°C for longer. ; Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.
• Shipping: Ambient
• Background: The beta-amyloid peptide (beta A4), proteolytically released from the amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimers disease. Cleavage of APP by alpha-secretase or alternatively by beta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is nonamyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59).

Reference Data