Analytical Data
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Gene name
DPYS
- Application
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Alternative Names
DPYS；Dihydropyrimidinase
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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
Q14117
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Expression Region
1-519aa
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AA Sequence
MAAPSRLLIR GGRVVNDDFS EVADVLVEDG VVRALGHDLL PPGGAPAGLR VLDAAGKLVL PGGIDTHTHM QFPFMGSRSI DDFHQGTKAA LSGGTTMIID FAIPQKGGSL IEAFETWRSW ADPKVCCDYS LHVAVTWWSD QVKEEMKILV QDKGVNSFKM FMAYKDLYMV TDLELYEAFS RCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV NCPLYIVHVM SKSAAKVIAD ARRDGKVVYG EPIAASLGTD GTHYWNKEWH HAAHHVMGPP LRPDPSTPDF LMNLLANDDL TTTGTDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW EKGVHSGKMD ENRFVAVTST NAAKIFNLYP RKGRIAVGSD ADIVIWDPKG TRTISAKTHH QAVNFNIFEG MVCHGVPLVT ISRGKVVYEA GVFSVTAGDG KFIPRKPFAE YIYKRIKQRD RTCTPTPVER APYKGEVATL KSRVTKEDAT AGTRKQAHP
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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
DPYS (Dipeptidyl Peptidase I) is a serine protease that plays a crucial role in the activation of various pro-enzyme forms of serine and cysteine peptidases, contributing to numerous physiological processes, including immune responses and protein metabolism. The study of DPYS has gained attention due to its involvement in the digestion of dietary proteins and possible implications in disease mechanisms, such as cancer and metabolic disorders. Researchers have begun to focus on recombinant DPYS proteins to explore their enzymatic properties, understand their structure-function relationships, and evaluate potential therapeutic applications. Advances in recombinant DNA technology have enabled the production of active DPYS variants in suitable expression systems, allowing researchers to conduct in-depth biochemical analyses and functional assays. These studies aim to elucidate how the modulation of DPYS activity might influence biological pathways and provide insights for developing novel therapeutic strategies. Understanding the nuances of DPYS function and regulation could lead to innovative approaches to treat conditions associated with dysregulated protein processing and enhance our knowledge of cellular regulatory mechanisms.
