Analytical Data
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Gene name
PARP16
- Application
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Alternative Names
ADP-ribosyltransferase diphtheria toxin-like 15;Poly [ADP-ribose] polymerase 16;PARP-16
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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
Q8N5Y8
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Expression Region
1-287 aa
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AA Sequence
MQPSGWAAAREAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELLQSSGDNHKRAWDLVSWILSSKVLTIHSAGKAEFEKIQKLTGAPHTPVPAPDFLFEIEYFDPANAKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSLFGEGTYLTSDLSLALIYSPHGHGWQHSLLGPILSCVAVCEVIDHPDVKCQTKKKDSKEIDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQKPPKRASSQLSWFS
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Molecular Weight
39.1 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
PARP16, a member of the poly(ADP-ribose) polymerase family, plays a significant role in cellular responses to stress and DNA damage. Initially recognized for its involvement in the regulation of protein quality and the endoplasmic reticulum (ER) stress response, PARP16 operates by catalyzing the addition of ADP-ribose moieties to target proteins, thereby influencing their activity and stability. Recent research has highlighted PARP16's involvement in various cellular processes, including apoptosis, autophagy, and inflammation, making it a critical player in both normal physiology and disease states. The aberration in PARP16 function has been linked to several pathologies, including neurodegenerative diseases and cancer, underscoring its potential as a therapeutic target. Investigating the mechanisms by which PARP16 interacts with other cellular pathways can provide deeper insights into its biological significance and therapeutic potential. Understanding the role of PARP16 in regulating cellular homeostasis and its response to external stressors is crucial, as it may unveil novel strategies for the treatment of diseases characterized by dysregulated cellular response mechanisms. Therefore, the recombinant expression and functional characterization of PARP16 are pivotal in elucidating its biochemical properties and interactions, paving the way for future studies aimed at harnessing its potential in biomedical applications.
