Analytical Data
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Gene name
APEH
- Application
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Alternative Names
Acyl-peptide hydrolase (APH) (Acylaminoacyl-peptidase) (Oxidized protein hydrolase) (OPH) (D3F15S2) (D3S48E) (DNF15S2)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P13798
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Expression Region
1-732aa
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Molecular Weight
85.2 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
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Protein Description
APEH (Acyl-Prolyl Endopeptidase Homolog) is an important enzyme implicated in various physiological processes, including protein metabolism and the modulation of cellular signaling pathways. Recent studies have highlighted its role in regulating inflammation and its potential involvement in neurodegenerative diseases and cancer. The enzyme's ability to cleave specific peptide bonds suggests that it may be crucial for the processing of bioactive peptides, which can impact numerous biological functions. Given the rising interest in proteomics and peptide-based therapeutics, understanding the structure and function of APEH has significant implications for drug development and therapeutic interventions. Research has focused on characterizing the enzyme’s catalytic mechanism, substrate specificity, and its interactions with other biomolecules. By utilizing advanced techniques such as X-ray crystallography and cryo-electron microscopy, scientists aim to elucidate the three-dimensional structure of APEH, which is essential for understanding its enzymatic activity and regulation. Additionally, investigating APEH's expression patterns in various tissues and its potential as a biomarker for disease states can provide insights into its physiological relevance. This multifaceted approach not only sheds light on the enzyme’s biological significance but also paves the way for innovative strategies in treating diseases associated with dysregulated peptide processing. As research continues, APEH stands out as a promising target for future studies aimed at unraveling the complex interplay of enzymes in health and disease.
