Recombinant Full Length Tetraodon Fluviatilis Amyloid Beta A4 Protein(App) Protein, His-Tagged

• Cat.No.: RFL-14031TF
• Product Overview: Recombinant Full Length Tetraodon fluviatilis Amyloid beta A4 protein(app) Protein (O73683) (19-780aa), fused to N-terminal His tag, was expressed in E. coli.

Specification

• Source: E.coli expression system
• Species: Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis)
• Tag: His
• Form: Lyophilized powder
• Protein length: Full Length of Mature Protein (19-780)
• AA Sequence: AEVPTDVSMGLLAEPQVAMFCGKIN MHINVQSGKWEPDPSGTKSCIGTKE GILQYCQEVYPELQITNVVEANQPV SIQNWCKKGRKQCRSHMHIVVPYRC LVGEFVSDALLVPDKCKFLHQERMN QCESHLHWHTVAKESCGDRAMNLHD YGMLLPCGIDRFRGVEFVCCPAEAE RDMDSTEKDADDSDVWWGGADNDYS DNSMVREPEPAEQQEETRPSVVEEE EEGEVAQEDDEEEEEVLDTDQDGDG EEDHEAADDEEEEEDVDEIDAFGES DDVDADEPTTNVAMTTTTTTTTTES VEEVVRMFCWAHADTGPCTASMPSW YFDAVDGRTMYELMYGGCGGNMNNF ESEEYCLSVCSSVVPTDMPSSPDAV DHYLETPADENEHAHFQKAKESLEA KHRERMSQVMREWEEAERQAKNLPR ADKKIVIQRFQEKVEALEQEAASER QQLVETHMARVEALLNDRRRLALEN YLTALQQDPPRPRHVFSLLKKYVRA EQKDRQHTLKHFEHVRMVDPKKAAQ IRPQVLTHLRVIEERMNQSLGLLYK VPGVADDIQDQVELLQREQAEMAQQ LANLQTDVRVSYGNDALMPDQELGD GQADLLPQEDTLGGVGFVHPESFNQ LNTENQVEPVDSRPTFERGVPTRPV TGKSMEAVPELRMETEDRQSTEYEV HHQKLVFFAEDVGSNKGAIIGLMVG GVVIATVIVITLVMLRKKQYTSIHH GIIEVDAAVTPEERHLSKMQQNGYE NPTYKFFEQMQN
• Purity: Greater than 90% as determined by SDS-PAGE.
• Applications: SDS-PAGE
• Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
• Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
• Storage Buffer: Tris/PBS-based buffer, 6% Trehalose, pH 8.0
• Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
• Gene Name: app
• Synonyms: app; Amyloid-beta A4 protein; ABPP; APP; Alzheimer disease amyloid A4 protein homolog; Amyloid precursor protein; Amyloid-beta precursor protein
• UniProt ID: O73683

Gene Information

• Gene Name: app
• Synonyms: app; Amyloid-beta A4 protein; ABPP; APP; Alzheimer disease amyloid A4 protein homolog; Amyloid precursor protein; Amyloid-beta precursor protein
• UniProt ID: O73683

Reviews

11/19/2021

This can be advantageous in understanding disease mechanisms and developing novel therapeutics.

07/28/2019

APP protein is highly recommended for various research applications, including ELISA and protein electron microscopy structure analysis.

12/23/2017

The manufacturer can provide detailed documentation on the quality control measures undertaken during protein production and purification.

04/29/2016

APP protein might have biomarker properties, meaning its levels or activity could be indicative of disease progression or treatment response.

Q&As

Are there any ongoing research efforts targeting the APP protein for Alzheimer's disease treatment?

Yes, 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.

How does the APP protein contribute to synaptic dysfunction in Alzheimer's disease?

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.

Are there any potential therapeutic strategies targeting APP protein dysregulation?

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.

How is the APP protein processed and cleaved in the brain?

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.

Are there any therapeutic strategies targeting the APP protein in Alzheimer's disease?

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.

Are there any non-genetic factors that can influence APP protein dysregulation?

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.

Can imaging techniques detect amyloid-beta plaques in the brain?

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.

Can the APP protein be targeted for diagnostic purposes?

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.

Is the APP protein involved in any other diseases or conditions?

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.

Are there any known risk factors associated with APP protein dysregulation?

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.

Can changes in APP protein expression or processing be detected in animal models of Alzheimer's 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.

Can the APP protein be measured in biological samples for diagnostic purposes?

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.

What are the potential functions of amyloid-beta produced from APP cleavage?

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.

Does the APP protein have any known physiological roles outside the brain?

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.

Are there any known compounds or drugs that can modulate APP protein expression or processing?

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.

Are there any genetic mutations or variants associated with the APP gene?

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.

How is the expression or processing of APP protein regulated?

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.

How is the APP protein associated with Alzheimer's disease?

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.