Analytical Data
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Gene name
DNPEP
- Application
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Alternative Names
DNPEP；ASPEP；DAP；Aspartyl aminopeptidase
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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
Q9ULA0
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Expression Region
1-475aa
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AA Sequence
MQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD
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Molecular Weight
68.4 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
Related Products
Protein Description
DNPEP (Dipeptidase) is an important enzyme involved in the hydrolysis of dipeptides, playing a crucial role in protein metabolism and amino acid absorption in various biological systems. Research on DNPEP has gained significance in recent years due to its potential implications in human health and disease. Dysregulation of dipeptide metabolism has been linked to metabolic disorders, neurodegenerative diseases, and various cancers, highlighting the need for a better understanding of this enzyme’s function and regulation. The recombinant expression of DNPEP allows for the production of large quantities of the enzyme, facilitating detailed biochemical studies. By utilizing advanced molecular biology techniques, researchers aim to elucidate the structure-function relationship of DNPEP, investigate its catalytic mechanisms, and explore its interactions with substrates and inhibitors. Such studies not only enhance our understanding of DNPEP’s role in physiology but may also unveil novel therapeutic targets for diseases associated with dipeptide metabolism. The growing interest in DNPEP research reflects its potential for contributing to biomedical advancements and improving therapeutic strategies for metabolic and neurodegenerative conditions.
