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Key Documents

MAB343

Sigma-Aldrich

Anti-APP Antibody, APP 643-695 CT fragment, clone 2.F2.19B4

ascites fluid, clone 2.F2.19B4, Chemicon®

别名:

APP, Jonas clone

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About This Item

分類程式碼代碼:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物源

mouse

品質等級

抗體表格

ascites fluid

無性繁殖

2.F2.19B4, monoclonal

物種活性

rat, human

製造商/商標名

Chemicon®

技術

immunohistochemistry: suitable (paraffin)
western blot: suitable

同型

IgG1

UniProt登錄號

運輸包裝

dry ice

目標翻譯後修改

unmodified

基因資訊

human ... APP(351)

特異性

Reacts with intact full-length Alzheimer precursor protein (APP) and selectively with the cytoplasmic carboxyl fragment of APP 643-695. Epitope has reportedly been mapped in this paper http://www.impub.co.uk/abs/W386.html

免疫原

Carboxyl fragment of APP 643-695 / Jonas.
Epitope: APP 643-695 C-terminal fragment

應用

Immunohistochemistry on paraffin sections: 10-20 μg/mL * See protocol below.

Western blot: 10 μg/mL

Optimal working dilutions must be determined by end user.

APPLICATION NOTES FOR MAB343

IMMUNOHISTOCHEMISTRY

1) Prepare paraformaldehyde-fixed paraffin sections. Wash twice for 5 min in xylene to deparaffinize. Wash sections for 5 min in a descending series of alcohol solutions (100%, 96%, 90%, 80%, 70%, 50%, 30%).

2) Wash sections 3 times in distilled water.

3) Wash in TBS (50 mM Tris-HCl, 150 mM NaCl, pH 7.6). To block endogenous peroxidase wash with methanol containing 0.6% H2O2 (v/v) and 10 % horse serum (v/v) for 5 min at room temperature.

4) Wash sections for 5 min in TBS.

5) Incubate sections with MAB343 (diluted in TBS containing 10% horse serum (v/v)) overnight at +4°C or for 2 hours at 37°C in a humid chamber.

6) Wash sections 3 times in TBS for 5 min..

7) Detect with standard secondary antibody detection system (PAP, ABC, etc.).

8) Wash sections in TBS.

9) Embed sections and examine.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
This Anti-APP Antibody, APP 643-695 C-terminal fragment, clone 2.F2.19B4 is validated for use in IH(P), WB for the detection of Alzheimer Precursor Protein.

外觀

Unpurified
Liquid.

儲存和穩定性

Maintain lyophilized material at +2–8°C for up to 12 months. After reconstitution maintain frozen at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles.

分析報告

Control
Brain

其他說明

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

法律資訊

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

免責聲明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析证书(COA)

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Eun Mi Hwang et al.
Bioorganic & medicinal chemistry, 16(14), 6669-6674 (2008-06-21)
In order to access beta-secretase (BACE1), and enzyme strongly implicated in the cause of Alzheimer's disease, inhibitors must possess sufficient lipophilicity to traverse two lipid bilayers. Current drug candidates, which are almost totally peptide-derived, are thus inefficient because cell permeability
Gregory D Van Vickle et al.
Biochemistry, 46(36), 10317-10327 (2007-08-21)
We investigated the morphology and biochemistry of the amyloid-beta (Abeta) peptides produced in TgCRND8 Tg mice carrying combined amyloid precursor protein (APP) Swedish (K670M/N671L) and Indiana (V717F) mutations. Histological analyses employing amyloid-specific staining and electron microscopy revealed that the TgCRND8
Effects of peptides derived from BACE1 catalytic domain on APP processing.
Seung Woo Yeon, Yong-Jin Jeon, Eun Mi Hwang, Tae-Yong Kim
Peptides null
A TAG1-APP signalling pathway through Fe65 negatively modulates neurogenesis.
Quan-Hong Ma, Toshitaka Futagawa, Wu-Lin Yang, Xiao-Dan Jiang, Li Zeng, Yasuo Takeda et al.
Nature Cell Biology null
P Ponte et al.
Nature, 331(6156), 525-527 (1988-02-11)
The amyloid proteins isolated from neuritic plaques and the cerebrovasculature of Alzheimer's disease are self-aggregating moieties termed A4 protein and beta-protein, respectively. A putative A4 amyloid precursor (herein termed A4(695] has been characterized by analysis of a human brain complementary

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