Analytical Data
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Gene name
DDP1
- Application
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Alternative Names
DDP1；DDP；DDP1；TIM8A；Mitochondrial import inner membrane translocase subunit Tim8 A
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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
Q99321
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Expression Region
2-188aa
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AA Sequence
GKTADNHGPVRSETAREGRENQVYSPVTGARLVAGCICLTPDKKQVLMITSSAHKKRWIVPKGGVEKDEPNYETTAQRETWEEAGCIGKIVANLGTVEDMRPPKDWNKDIKQFENSRKDSEVAKHPPRTEFHFYELEIENLLDKFPECHKRHRKLYSYTEAKQNLIDAKRPELLEALNRSAIIKDDK
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Molecular Weight
37.4 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
DDP1 (Dipeptidyl Peptidase I) is a serine peptidase that plays a crucial role in various physiological processes, including immune responses and tissue remodeling. Research on DDP1 has gained momentum due to its involvement in the activation of other proteolytic enzymes, which are significant for processing bioactive peptides and proteins. Abnormal functioning of DDP1 has been linked to several pathological conditions, including inflammatory diseases and cancers. The cloning and expression of recombinant DDP1 in heterologous systems allow for the detailed study of its enzymatic properties, substrate specificity, and regulatory mechanisms. This research is particularly important for developing targeted therapeutics that can modulate DDP1 activity, providing opportunities for novel treatment strategies in diseases where dysregulated proteolytic activity is a contributing factor. Recombinant protein technology enables the production of DDP1 in sufficient quantities for structural and functional analyses, paving the way for understanding its role in health and disease. Additionally, exploring DDP1's interaction with inhibitors and activators contributes to the broader field of enzyme regulation, offering insights that could lead to the design of new pharmacological agents.
