Cat. # | Size | Qty. | Price |
---|---|---|---|
9784T | 1 Kit (8 x 20 microliters) |
|
Product Includes | Quantity | Applications | Reactivity | MW(kDa) | Isotype |
---|---|---|---|---|---|
β-Amyloid (D54D2) XP® Rabbit mAb 8243 | 20 µl |
|
H | 5 | Rabbit IgG |
Neurofilament-L (C28E10) Rabbit mAb 2837 | 20 µl |
|
H M R | 70 | Rabbit IgG |
Tau (Tau46) Mouse mAb 4019 | 20 µl |
|
H M R | 50-80 | Mouse IgG1 |
BACE1 (D10E5) Rabbit mAb 5606 | 20 µl |
|
H M R | 70 | Rabbit IgG |
APP/β-Amyloid (NAB228) Mouse mAb 2450 | 20 µl |
|
H Mk B | 100 to 140 | Mouse IgG2a |
α-Synuclein (Syn204) Mouse mAb 2647 | 20 µl |
|
H | 18 | Mouse IgG2a |
GSK-3α/β (D75D3) Rabbit mAb 5676 | 20 µl |
|
H M R Hm Mk | 51, 46 | Rabbit IgG |
Phospho-GSK-3α (Ser21) (36E9) Rabbit mAb 9316 | 20 µl |
|
H M R Mk | 51 | Rabbit |
Anti-rabbit IgG, HRP-linked Antibody 7074 | 100 µl |
|
Goat | ||
Anti-mouse IgG, HRP-linked Antibody 7076 | 100 µl |
|
Horse |
Product Information
Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human ß-amyloid peptide (Aß), surrounding Glu450 of human Neurofilament-L protein, native bovine tau protein (carboxy terminus), a synthetic peptide corresponding to residues surrounding Asp490 of human BACE1 protein, human recombinant α-synuclein protein (amino terminus), ß-amyloid protein (amino terminus) (Lee et al., 2003), a synthetic peptide surrounding Gln269 of human GSK-3α protein, or a synthetic phosphopeptide corresponding to residues surrounding Ser21 of human GSK-3α protein
Alzheimer's Disease (AD) is one of the most common neurodegenerative diseases worldwide. Clinically, it is characterized by the presence of extracellular amyloid plaques and intracellular neurofibrillary tangles, which results in neuronal dysfunction and cell death. Central to this disease is the differential processing of the integral transmembrane glycoprotein Amyloid β (A4) precursor protein (APP) 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). β-secretase (BACE) is an aspartic acid proteinase that catalyses the initial step in APP processing by cleaving and releasing a soluble, extracellular APP-β (sAPPβ) ectodomain and generating a membrane-bound, carboxy-terminal fragment consisting of 99 amino acids (CTF99). Additional processing of CTF99 by γ-secretase generates the amyloid β-peptide (Aβ) that forms aggregates in the brains of AD patients. BACE is an attractive target for inhibitors in AD therapy since it catalyses the first and rate limiting step in amyloidogenic APP processing (2). Pro-BACE-1 is synthesized in the ER before it is transported to the trans-Golgi network to undergo maturation (3). The extracellular deposition and accumulation of the released Aβ fragments and an α-synuclein fragment known as the non- Aβ fragment, form the main components of amyloid plaques in AD. GSK-3α regulates the production of Aβ peptides. Administration of therapeutic concentrations of lithium, a GSK-3 inhibitor, attenuates Aβ production by specifically inhibiting the cleavage of APP by γ-secretase, thereby blocking accumulation of Aβ peptides in the brains of mice that overproduce APP (4). AD is also characterized by the presence of neurofibrillary tangles. These tangles are the result of hyperphosphorylation and oligomerization of the microtubule associated protein Tau and lead to apoptosis of the neuron. In particular, phosphorylation of Tau Ser396 by GSK-3 or CDK5 destabilizes microtubules in AD (5,6). Additionally, neurofilaments are the major intermediate filaments found in neurons and consist of light (NFL), medium (NFM) and heavy (NFH) subunits (7). Accumulation of neurofilaments are found in many human neurological disorders including AD (7).
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