Analytical Data
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Gene name
APP
- Application
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Alternative Names
APP；KIAA0228；PAT1；Amyloid Protein-binding Protein 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05067
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Expression Region
18-339aa
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AA Sequence
RSRPSFHPVSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCGTFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDQYWEKI
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Molecular Weight
37.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research on the recombinant protein of amyloid precursor protein (APP) has gained significant attention due to its implications in neurodegenerative diseases, particularly Alzheimer's disease (AD). APP is a membrane-bound protein that plays a crucial role in neuronal growth, survival, and synaptic function. However, its improper cleavage by secretases leads to the generation of amyloid-beta (Aβ) peptides, which aggregate to form plaques in the brains of AD patients, contributing to neurotoxicity and neurodegeneration. Understanding the structure and function of APP and its cleavage products is essential for developing therapeutic strategies aimed at reducing Aβ accumulation. Recombinant techniques enable the production of APP and its derivatives, facilitating the study of their biological properties and interactions. By employing molecular cloning and expression systems, researchers can generate large quantities of these proteins for in vitro and in vivo studies, ultimately contributing to a better understanding of AD pathology. This research not only enhances our knowledge of APP's role in the central nervous system but also opens doors for designing targeted interventions that could mitigate the progression of Alzheimer's disease. As such, the study of recombinant APP is a vital area of exploration in the quest for effective AD treatments, yielding insights that could revolutionize our approach to managing this complex and challenging condition.
