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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
β-Amyloid (D54D2) XP® Rabbit mAb 8243 40 µl
H M 5 Rabbit IgG
Neurofilament-L (C28E10) Rabbit mAb 2837 40 µl
H M R 70 Rabbit IgG
Tau (Tau46) Mouse mAb 4019 40 µl
H M R 50 to 80 Mouse IgG1
BACE (D10E5) Rabbit mAb 5606 40 µl
H M R 70 Rabbit IgG
APP/β-Amyloid (NAB228) Mouse mAb 2450 40 µl
H Mk B 100 to 140 Mouse IgG2a
α-Synuclein (Syn204) Mouse mAb 2647 40 µl
H 18 Mouse IgG2a
GSK-3α/β (D75D3) XP® Rabbit mAb 5676 40 µl
H M R Hm Mk 51, 46 Rabbit IgG
Phospho-GSK-3α (Ser21) (36E9) Rabbit mAb 9316 40 µl
H M R Mk 51 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
All Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl
All Horse 

Product Description

The Alzheimer Disease Antibody Sampler Kit provides an economical means of evaluating Alzheimer Disease-related signaling. The kit contains enough primary and secondary antibodies to perform four western blot experiments per primary antibody.


Specificity / Sensitivity

β-Amyloid (D54D2) XP® Rabbit mAb recognizes endogenous levels of total β-amyloid peptide (Aβ). The antibody detects several isoforms of Aβ, such as Aβ-37, Aβ-38, Aβ-39, Aβ-40, and Aβ-42. APP/β-Amyloid (NAB228) Mouse mAb detects endogenous levels of APP/β-Amyloid protein. Although this antibody recognizes both the phospho and non-phospho forms of the protein, it has been shown to prefer the phosphorylated form in some systems. BACE (D10E5) Rabbit mAb detects endogenous levels of total BACE protein. Phospho-GSK-3α (Ser21) (36E9) Rabbit mAb detects endogenous levels of GSK-3α protein when phosphorylated at Ser21, and does not detect GSK-3β when phosphorylated at Ser9. GSK-3α/β (D75D3) XP® Rabbit mAb detects endogenous levels of total GSK-3α and GSK-3β protein. The antigen is 100% conserved between GSK-3α and GSK-3β in humans, monkeys, mice, and rats. Neurofilament-L (C28E10) Rabbit mAb detects endogenous levels of total Neurofilament-L protein. α-Synuclein (Syn204) Mouse mAb detects endogenous levels of total synuclein protein. This antibody detects recombinant α but not β-synuclein (Giasson, B.I. et al., 2000). Tau (Tau46) Mouse mAb detects endogenous levels of total tau protein, and also cross-reacts with MAP2 at 280 kDa. This antibody is predicted to detect all six isoforms of tau based on the amino acid sequence.


Source / Purification

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 BACE 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 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).


1.  Selkoe, D.J. (1996) J Biol Chem 271, 18295-8.

2.  Hunt, C.E. and Turner, A.J. (2009) FEBS J 276, 1845-59.

3.  Johnson , G.V. and Stoothoff , W.H. (2004) J. Cell Sci. 117, 5721-5729.

4.  Walter, J. et al. (2001) J Biol Chem 276, 14634-41.

5.  Bramblett, G. T. et al. (1993) Neuron 10, 1089-1099.

6.  Phiel, C.J. et al. (2003) Nature 423, 435-9.

7.  Al-Chalabi, A. and Miller, C.C. (2003) Bioessays 25, 346-55.


Entrez-Gene Id 351, 23621, 2931, 2932, 4747, 6622, 4137
Swiss-Prot Acc. P05067, P56817, P49840, P49841, P07196, P37840, P10636-8


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.