Analytical Data
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Gene name
DNPH1
- Application
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Alternative Names
C6orf108; RCL
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43598-1
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Expression Region
A2-T174
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Protein Length
Full Length of Isoform-1
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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
DNPH1, or Dipeptidyl Peptidase-like Protein 1, is a protein that has garnered significant interest in the field of molecular biology and biochemistry due to its role in various cellular processes. It is primarily associated with regulating metabolic pathways and has been implicated in the modulation of immune responses and cell signaling. Current research indicates that DNPH1 is involved in the processing of peptides, which is essential for the presentation of antigens and the activation of T cells. Moreover, aberrations in DNPH1 expression have been linked to various diseases, including metabolic disorders and cancers. Given its potential as a therapeutic target, the recombinant expression of DNPH1 has become a focal point for researchers aiming to elucidate its structure-function relationship and biological significance. By producing and analyzing recombinant DNPH1, scientists aim to better understand its enzymatic activity, substrate specificity, and interaction with other cellular components. Such studies may pave the way for novel therapeutic interventions, especially in conditions where DNPH1 dysregulation contributes to disease pathology. This research not only expands our understanding of DNPH1 but also provides insight into its potential roles in health and disease.
