Analytical Data
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Gene name
OPLAH
- Application
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Alternative Names
5-oxo-L-prolinase;5-OPase;Pyroglutamase
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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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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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 (O-linked N-acetylglucosamine phosphatase) is an essential enzyme involved in the regulation of O-linked N-acetylglucosamine (O-GlcNAc) modifications on serine and threonine residues of proteins, which play a crucial role in various cellular processes, including signal transduction, transcription, and stress responses. The dysregulation of O-GlcNAcylation has been linked to several diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, highlighting the importance of understanding this regulatory mechanism. Recent advancements in structural biology and biochemistry have facilitated the characterization of OPLAH, revealing insights into its catalytic mechanism, substrate specificity, and interactions with other cellular components. Researchers are increasingly focusing on the potential therapeutic implications of targeting OPLAH for modulating O-GlcNAc levels in diseased states, making it a promising candidate for drug discovery. Additionally, studies employing cellular models and animal systems are investigating the role of OPLAH in disease progression and its potential as a biomarker. The ongoing exploration of OPLAH and its regulatory networks continues to deepen our understanding of cellular homeostasis and pathology.
