Human Amyloid beta A4 protein (Fc Tag)

Human Amyloid beta A4 protein (Fc Tag)

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• Material Safety Data Sheets (MSDS)

Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.

Amyloid beta A4 protein

CVAP; AG; CTFGAMMA; ABETA; APPI; AD1; APPICAN; BETAAPP; ADAP; PN-II; AL024401; AAA; ABPP; E030013M08RIK; PROTEASE NEXIN II; PN2

P05067

APP; A4; AD1

Human Cells

A DNA sequence encoding the human APP-751 isoform (NP_958816.1) (Met 1-Leu 669) was expressed with the C-terminal fused Fc region of human IgG1.

Human

The recombinant human APP/Fc is a disulfide-linked homodimeric protein after removal of the signal peptide. The reduced monomer consists of 890 amino acids and predicts a molecular mass of 101 kDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rhAPP/Fc monomer is approximately 150-160 kDa due to the glycosylation.

> 95 % as determined by SDS-PAGE

Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2, (R&D Systems, Catalog # ES002). The IC50 value is < 1.2 nM.