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Western blot analysis of APP-BP1 on a RSV-3T3 cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti- APP-BP1 antibody.


BD Transduction Laboratories™ Purified Mouse Anti- APP-BP1

Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Amyloid precursor protein (APP) gene encodes multiple APPs ranging from 695 to 770 amino acids. These proteins are processed into β-Amyloid peptides (39-43 amino acids), which form abnormal plaques in the cerebral cortex and blood vessel walls during Alzheimer's disease. The transmembrane form of APP is a putative cell surface receptor that possesses neurite-promoting activity, co-localizes with the plaques found in Alzheimer's disease, and is involved in synaptic vesicle recycling. APP binding protein 1 (APP-BP1) interacts with the C-terminus of APP, and is a relative of the ubiquitin-activating enzymes (E1). The structure of APP-BP1 includes a human Uba3 binding site (UBS) at amino acids 443 to 479. This site may be important for APP-BP1 regulation of the cell cycle through interactions with ubiquitinylation-related pathways. Transfection of APP-BP1 in cells with a ts41 mutation suppresses the abnormal S-phases observed in these cells in a hUba3- and hUbc12-dependent manner. In addition, APP-BP1 has been implicated in ubiquitinylation-dependent apoptosis in neurons. Thus, APP-BP1 may be a multi-functional APP-binding protein that regulates cell cycle dynamics.
Development References (3)
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Chen Y, McPhie DL, Hirschberg J, Neve RL. The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons. J Biol Chem. 2000; 275(12):8929-8935. (Biology). View Reference
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Chow N, Korenberg JR, Chen XN, Neve RL. APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J Biol Chem. 1996; 271(19):11339-11346. (Biology). View Reference
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Hori T, Osaka F, Chiba T. Covalent modification of all members of human cullin family proteins by NEDD8. Oncogene. 1999; 18(48):6829-6834. (Biology). View Reference
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