Analytical Data
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Gene name
DPP7
- Application
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Alternative Names
DPP7；DPP2；QPP；Dipeptidyl peptidase 2
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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
Q9UHL4
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Expression Region
26-492aa
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AA Sequence
APDPG FQERFFQQRL DHFNFERFGN KTFPQRFLVS DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA LLVFAEHRYY GKSLPFGAQS TQRGHTELLT VEQALADFAE LLRALRRDLG AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA GALAASAPVL AVAGLGDSNQ FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR WEFGTCQPLS DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ ACTEINLTFA SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW GGDLRAASNI IFSNGNLDPW AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS HPEDPASVVE ARKLEATIIG EWVKAARREQ QPALRGGPRL SL
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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 7 (DPP7) is a member of the dipeptidyl peptidase family, which plays a crucial role in regulating various biological processes, including inflammation, immune response, and metabolic pathways. Research on DPP7 has gained attention due to its potential involvement in several diseases, such as cancer, diabetes, and autoimmune disorders. The enzyme is known to cleave and inactivate bioactive peptides, thereby modulating their physiological effects. Understanding the structure and function of DPP7 is essential for elucidating its mechanisms of action in health and disease. The production of recombinant DPP7 protein has emerged as a valuable tool for studying its enzymatic activity, binding interactions, and physiological roles in vitro and in vivo. This research can pave the way for the development of novel therapeutics that target DPP7, enhancing disease management strategies and improving patient outcomes. Through the exploration of DPP7's structure-function relationship, scientists aim to uncover its potential as a biomarker for disease progression and therapeutic target, contributing to the broader understanding of peptide metabolism and its implications in human health.
