Recombinant Human APP protein, GST-tagged
Cat.No. : | APP-721H |
Product Overview : | Human APP full-length ORF ( AAH04369.1, 19 a.a. - 305 a.a.) recombinant protein with GST-tag at N-terminal. |
- Specification
- Gene Information
- Related Products
Description : | This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. In addition, two of the peptides are antimicrobial peptides, having been shown to have bacteriocidal and antifungal activities. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Aug 2014] |
Source : | Wheat Germ |
Species : | Human |
Tag : | GST |
Molecular Mass : | 57.31 kDa |
AA Sequence : | EVPTDGNAGLLAEPQIAMFCGRLNM HMNVQNGKWDSDPSGTKTCIDTKEG ILQYCQEVYPELQITNVVEANQPVT IQNWCKRGRKQCKTHPHFVIPYRCL VGEFVSDALLVPDKCKFLHQERMDV CETHLHWHTVAKETCSEKSTNLHDY GMLLPCGIDKFRGVEFVCCPLAEES DNVDSADAEEDDSDVWWGGADTDYA DGSEDKVVEVAEEEEVAEVEEEEAD DDEDDEDGDEVEEEAEEPYEEATER TTSIATTTTTTTESVEEVVREKWYK EVHSGQARWLML |
Applications : | Enzyme-linked Immunoabsorbent Assay; Western Blot (Recombinant protein); Antibody Production; Protein Array |
Notes : | Best use within three months from the date of receipt of this protein. |
Storage : | Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing. |
Storage Buffer : | 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. |
Gene Name : | APP amyloid beta (A4) precursor protein [ Homo sapiens ] |
Official Symbol : | APP |
Synonyms : | APP; amyloid beta (A4) precursor protein; AD1, Alzheimer disease; amyloid beta A4 protein; peptidase nexin II; preA4; protease nexin-II; peptidase nexin-II; beta-amyloid peptide; alzheimer disease amyloid protein; cerebral vascular amyloid peptide; AAA; AD1; PN2; ABPP; APPI; CVAP; ABETA; PN-II; CTFgamma; |
Gene ID : | 351 |
mRNA Refseq : | NM_000484 |
Protein Refseq : | NP_000475 |
MIM : | 104760 |
UniProt ID : | P05067 |
Products Types
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◆ Lysates | ||
APP-3087HCL | Recombinant Human APP cell lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
Inquiry
- Q&As
- Reviews
Q&As (18)
Ask a questionYes, there is ongoing research focused on developing therapies that target the APP protein and its associated pathways in Alzheimer's disease. These include clinical trials investigating the effectiveness of anti-amyloid antibodies, small molecule inhibitors of amyloid-beta production, and modulators of APP processing enzymes. Additionally, other approaches targeting downstream processes related to APP or amyloid-beta toxicity are also being explored.
The excessive accumulation of amyloid-beta peptides in Alzheimer's disease leads to synaptic dysfunction and loss. Amyloid-beta can disrupt neurotransmitter signaling, impair synaptic plasticity, and induce inflammation, ultimately leading to cognitive impairment and memory deficits commonly observed in Alzheimer's disease.
Yes, there are various therapeutic strategies being explored to target APP protein dysregulation in Alzheimer's disease. One approach is to reduce the production or aggregation of amyloid-beta, which is derived from APP cleavage. This can be done through the use of small molecule inhibitors or antibodies that target the enzymes involved in APP cleavage or amyloid-beta aggregation. Another approach is to modulate the expression or processing of APP itself, aiming to reduce the production of amyloid-beta.
The APP protein can undergo two main pathways of processing. The non-amyloidogenic pathway involves the cleavage of APP by alpha-secretase, producing soluble APP-alpha (sAPPα) and preventing the formation of amyloid-beta. The amyloidogenic pathway involves sequential cleavage by beta-secretase and gamma-secretase, resulting in the generation of amyloid-beta peptides of various lengths.
Numerous therapeutic strategies have been explored to target the APP protein and the production of amyloid-beta in Alzheimer's disease. These include inhibiting the enzymes responsible for amyloid-beta formation (beta-secretase and gamma-secretase), immunotherapies targeting amyloid-beta, and modulating APP processing and trafficking.
Yes, certain lifestyle and environmental factors have been associated with increased APP protein dysregulation. For example, chronic oxidative stress, inflammation, and metabolic dysfunction can impact APP processing and amyloid-beta production. Additionally, lifestyle choices such as a sedentary lifestyle, poor diet, and chronic stress may also contribute to APP dysregulation and the risk of developing Alzheimer's disease.
Yes, there are several imaging techniques, such as positron emission tomography (PET) using specific radioactive tracers, that can detect and quantify amyloid-beta plaque deposition in the brain. These imaging modalities are clinically used to support the diagnosis of Alzheimer's disease and monitor disease progression.
While the measurement of APP protein levels or its cleavage products in biological samples has shown promise as a diagnostic tool for Alzheimer's disease, it is not currently used in routine clinical practice. The sensitivity and specificity of these measurements need to be further improved to ensure their accuracy and reliability for diagnostic purposes.
Besides its role in Alzheimer's disease, the APP protein has been implicated in other neurodegenerative disorders such as Down syndrome and cerebral amyloid angiopathy. Additionally, it may play a role in certain types of cancers, as altered APP expression has been observed in some tumors.
While genetic mutations in the APP gene are associated with familial Alzheimer's disease, there are also other risk factors that can influence APP protein dysregulation. Age is the most significant risk factor, as the incidence of Alzheimer's disease increases with age. Other factors such as genetic variations in other genes, lifestyle choices (e.g., smoking, diet, exercise), and environmental factors may also contribute to APP protein dysregulation and the development of the disease.
Yes, animal models of Alzheimer's disease play an important role in studying changes in APP protein expression and processing. These models mimic certain aspects of Alzheimer's disease pathology, enabling researchers to investigate the effects of genetic and environmental manipulations on APP metabolism and amyloid-beta production. They help in understanding disease mechanisms and testing potential therapeutic interventions.
Yes, the measurement of APP protein or its cleavage products can be performed in cerebrospinal fluid (CSF) and blood samples. These measurements are explored for their potential diagnostic value and monitoring disease progression in Alzheimer's disease. However, they are not currently used as routine diagnostic tools due to limitations in sensitivity and specificity.
The functional role of amyloid-beta peptides is not entirely clear. Some studies suggest that amyloid-beta may have antimicrobial properties, play a role in synaptic activity, or act as a neuroprotectant. However, it is thought that abnormal accumulation of amyloid-beta contributes to neurotoxicity and neurodegeneration in Alzheimer's disease.
Yes, the APP protein is not limited to the brain and has been found in various tissues and cell types throughout the body. While its function outside the brain is less understood, studies suggest its involvement in processes such as cell adhesion, wound healing, fertilization, and tissue repair. However, further research is needed to fully elucidate its physiological roles beyond the brain.
Several compounds and drugs have shown potential in modulating APP protein expression or processing in preclinical and clinical studies. Examples include gamma-secretase inhibitors, beta-secretase inhibitors, and anti-amyloid antibodies. However, the development of effective and safe therapeutic interventions targeting APP dysregulation remains an active area of research.
Yes, mutations or variations in the APP gene have been identified in some familial forms of Alzheimer's disease. These mutations can increase the production or accumulation of amyloid-beta plaques, leading to an earlier onset and more aggressive form of the disease.
The expression and processing of APP protein are regulated by various mechanisms. Transcriptional regulation plays a role in controlling APP expression, where different transcription factors can influence its production. Moreover, post-translational modifications, such as phosphorylation and glycosylation, can affect APP processing pathways. Enzymes involved in APP cleavage, including beta-secretase (BACE1) and gamma-secretase, are also regulated and can influence the generation of amyloid-beta.
In Alzheimer's disease, the APP protein undergoes abnormal processing, leading to the production and accumulation of amyloid-beta (Aβ) plaques in the brain. These plaques are a hallmark feature of the disease and are believed to contribute to neurodegeneration and cognitive decline.
Customer Reviews (4)
Write a reviewThis can be advantageous in understanding disease mechanisms and developing novel therapeutics.
APP protein is highly recommended for various research applications, including ELISA and protein electron microscopy structure analysis.
The manufacturer can provide detailed documentation on the quality control measures undertaken during protein production and purification.
APP protein might have biomarker properties, meaning its levels or activity could be indicative of disease progression or treatment response.
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