Anti-APP ΔC31 (specific to C-terminal APP Δ31) antibody, rabbit serum (SAC)
Product code74-110Size

100 µlStorage

Store 4℃ for short term For long term storage store at -20℃.
Aliquot to avoid repeated freezing and thawing.

Concentration

N/A

Buffer

0.05% sodium azide

PurityRabbit antiserum

ImmunogenSynthetic peptide corresponding to the C-terminus of the caspase 3-cleaved
human APP (aa 658-664 of human APP695).

IsotypeRabbit IgG

Reactivity

Specific to the C-terminal end of APP ΔC31 of human, mouse and rat.

Special notes

N/A

Application

1. Western blotting (dilution: 1/3,000-1/1,000)
2. Immunocytechemistry (dilution: 1/1,000-1/500)
3. ELISA
Other applicacatiotons have not been tested.

Background

The Alzheimer amyloid precursor protein (APP) is a transmembrane protein
whose abnormal processing is associated with the pathogenesis of Alzheimer’s
disease. APP695 lacking the protease inhibitor domain is the predominant formin neuronal tissues. APP695 is cleaved by caspases into the 664-residue amino(N)-terminal fragment that lacks the carboxyl C-terminal 31-residues (APP
ΔC31) and the 31-residues C-terminal fragment (APP-C31). APP

C31

potentially plays pathophysiological roles in neuronal death (ref.3). An antibody(named SAC) against the C-terminus of caspase 3-cleaved human APP695 (APP
ΔC31) was raised in rabbit.

Data Link

UniProtKB P05067

Please note: All products are FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC
PROCEDURES. NOT FOR MILITARY USE.
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Data Images: 74-110 Anti-APP ΔC31 (specific to C-terminal APP Δ31) antibody, rabbit serum (SAC)

12396 kD

Fig.1 Western blot analysis of APPΔC31 .
Human NT2 neurons (neurally differentiated human NT2 embryonic carcinoma cells) were infectedwith adenovirus vector expressing β-galactosidase (lane 1), wild-type APP (lane 2) or APPΔC31 (lane3).
Cell lysates were prepared 48 h after infection, and proteins were analyzed by Western blotting using
this antibody (SAC). Neurons overexpressing wild-type APP contained a 96 kD SAC-immunoreactive
fragment which was also detected in APPΔC31-overexpressing neurons.

Fig.2 Immunocytochemical analysis of APPΔC31. Generation of the caspase-cleaved fragment APP
ΔC31 within neurons induced by serum deprivation.
Neurally differentiated NT2 cells were cultured for 96 h in the absence of fetal calf serum. Cells weretriply labeled for MAP2, the neuronal marker microtubule-associated protein 2 (MAP2), chromosomal
DNA (Hoechst), and APPΔC31 (SAC). MAP2-immunopositive neurons with apoptotic nuclei (arrows)
are intensively immunostained with SAC antibody.

The MAP2 antibody was obtained fromChemicon (CA, USA)
References: This antibody was used in ref.3 and 4.
1. Kang HG et al. (1987) “The precursor of Alzheimer’s disease amyloid A4 protein resembles a cellsurface receptor.” Nature 325: 33-736 PMID: 2881207
2. Selkoe DJ (1994) “Normal and abnormal biology of the beta-amyloid precursor protein.” Annu.

Rev. Neurosci. 17: 489-517 PMID: 8210185
3. Nishimura I et al. (2002) “Cell death induced by a caspase-cleaved transmembrane fragment ofthe Alzheimer amyloid precursor protein.” Cell Death Differ. 9: 199-208 PMID: 11840170
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Fax. 81-6-6877-2336 info@bioacademia.co.jp https://www.bioacademia.co.jp/en/

4. Nishimura I et al. (2003) “Upregulation and antiapoptotic role of endogenous Alzheimer amyloid
precursor protein in dorsal root ganglion neurons.” Exp. Cell Res. 286: 241-251 PMID: 12749853
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BioAcademia,Inc. Tel. 81-6-6877-2335

Fax. 81-6-6877-2336 info@bioacademia.co.jp https://www.bioacademia.co.jp/en/