Product Pathways - Neuroscience
β-Amyloid (1-42 Specific) (D9A3A) Rabbit mAb #14974
|14974S||100 µl ( 10 western blots )||￥3,250.00 现货查询||购买询价|
|14974T||20 µl ( 2 western blots )||￥1,200.00 现货查询||购买询价|
|14974||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-F=Immunofluorescence (Frozen),
Species predicted to react based on 100% sequence homology: Mouse, Rat,
Specificity / Sensitivity
β-Amyloid (1-42 Specific) (D9A3A) Rabbit mAb recognizes endogenous levels of total Aβ-42 peptide. This antibody may cross-react with Aβ-43 peptide.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human β-amyloid (1-42) peptide.
Confocal immunofluorescent analysis of wild-type (left) and Tg2576 mouse model of Alzheimer's brain (right) using β-Amyloid (1-42 Specific) (D9A3A) Rabbit mAb (green) and β3-Tubulin (TU-20) Mouse mAb #4466 (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
Western blot analysis of human Aβ-37, Aβ-38, Aβ-39, Aβ-40, and Aβ-42 peptides (2.5 ng) using β-Amyloid (1-42 Specific) (D9A3A) Rabbit mAb (upper) and β-Amyloid (D54D2) XP® Rabbit mAb #8243 (lower).
Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).
- Selkoe, D.J. (1996) J Biol Chem 271, 18295-8.
- Caporaso, G.L. et al. (1992) Proc Natl Acad Sci USA 89, 3055-9.
- Hung, A.Y. and Selkoe, D.J. (1994) EMBO J 13, 534-42.
- Suzuki, T. et al. (1994) EMBO J 13, 1114-22.
- Ando, K. et al. (1999) J Neurosci 19, 4421-7.
- Iijima, K. et al. (2000) J Neurochem 75, 1085-91.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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