Analytical Data
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Gene name
OPLAH
- Application
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Alternative Names
OPLAH；5-oxoprolinase
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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
O14841
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Expression Region
209-302aa
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AA Sequence
RELGFTHVSLSSEAMPMVRIVPRGHTACADAYLTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSATTY
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Molecular Weight
17.4 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
OPLAH (Oligopeptide L-Amino Acid Hydrolase) is a recently characterized enzyme that plays a crucial role in the hydrolysis of oligopeptides into free amino acids. Seeking to understand its biological significance, researchers have focused on its structural properties and catalytic mechanisms. The enzyme is of particular interest due to its potential applications in biotechnology and medicine, especially in metabolic processes related to protein degradation. Previous studies have indicated that OPLAH is involved in various physiological processes, including nutrient absorption and cellular signaling, which highlights its importance in maintaining homeostasis in organisms. Additionally, understanding OPLAH's functionality can contribute to advancements in enzyme engineering, enabling the design of more efficient biocatalysts for industrial applications. The sequencing of its gene and characterization of its protein structure have paved the way for further investigations into its biochemical properties, substrates, and inhibitors. Consequently, ongoing research aims to elucidate the regulatory mechanisms governing OPLAH activity and its interaction with other cellular components, which could lead to novel therapeutic strategies for conditions associated with protein misfolding or dysfunction. As the scientific community continues to unveil the complexities of OPLAH's role in cellular metabolism, the enzyme is positioned as a key player in the broader context of proteomics and metabolic engineering, underscoring its significance in both fundamental research and applied sciences.
