Analytical Data
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Gene name
DPP8
- Application
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Alternative Names
DPP8; Dipeptidyl peptidase 8; DP8; Dipeptidyl peptidase IV-related protein 1; DPRP-1; Dipeptidyl peptidase VIII; DPP VIII; Prolyl dipeptidase DPP8
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6V1X1
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Expression Region
M1-I898
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Protein Length
Full Length
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Molecular Weight
103.4 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
Dipeptidyl peptidase 8 (DPP8) is a serine protease that belongs to the DPP family of enzymes, which play crucial roles in the regulation of various physiological processes, including immune response and metabolism. Unlike its well-studied homolog DPP4, DPP8 has remained relatively underexplored despite its potential implications in health and disease. Recent research highlights its involvement in regulating inflammatory responses and its potential impact on conditions such as cancer and metabolic disorders. The interest in DPP8 has surged due to its unique structural features, which may provide novel therapeutic targets. Furthermore, DPP8 is implicated in the cleavage of peptides that can influence cell signaling pathways, making it a critical player in maintaining cellular homeostasis. Understanding the function and mechanisms of DPP8 could lead to the development of new treatments for diseases associated with dysregulated peptidase activity. Current studies focus on the characterization of recombinant DPP8 protein to elucidate its enzymatic activity, substrate specificity, and potential interactions with other proteins. This research not only aims to clarify the biological functions of DPP8 but also to explore its potential as a biomarker or therapeutic target in various diseases.
