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![APP Protein (Trx Tag) (recombinant human)](https://www.biomol.com/media/image/4f/be/c6/E-PDEH100549-20_600x600.jpg)
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Item number | Size | Datasheet | Manual | SDS | Delivery time | Quantity | Price |
---|---|---|---|---|---|---|---|
E-PDEH100549.20 | 20 µg | - | - |
7 - 16 business days* |
248.00€
|
||
E-PDEH100549.100 | 100 µg | - | - |
7 - 16 business days* |
742.00€
|
If you have any questions, please use our Contact Form.
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
Sequence: Asp672-Asn770. Fusion tag: N-Trx Endotoxin: < 1.0 EU per µg of the protein as... more
Product information "APP Protein (Trx Tag) (recombinant human)"
Sequence: Asp672-Asn770. Fusion tag: N-Trx Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method Observed Molecular Mass: 35 kDa. Protein function: Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by beta- and gamma-secretase to produce the amyloid-beta-protein (Abeta, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer's disease (AD), while in the other pathway, alpha-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Abeta peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli. Protein function: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). 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. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). 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. [The UniProt Consortium]
Keywords: | , Recombinant Human APP Protein(Trx Tag) |
Supplier: | Elabscience |
Supplier-Nr: | E-PDEH100549 |
Properties
Conjugate: | No |
Host: | E.coli |
Species reactivity: | human |
Format: | Lyophilized |
Database Information
KEGG ID : | K04520 | Matching products |
UniProt ID : | P05067 | Matching products |
Gene ID | GeneID 351 | Matching products |
Handling & Safety
Storage: | -80°C |
Shipping: | -20°C (International: -20°C) |
Caution
Our products are for laboratory research use only: Not for administration to humans!
Our products are for laboratory research use only: Not for administration to humans!
Information about the product reference will follow.
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