Analytical Data
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Gene name
PARP1
- Application
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Alternative Names
PARP1; ADPRT; ADPRT1; PPOL; pADPRT-1; ADP-ribosyltransferase diphtheria toxin-like 1; NAD(+) ADP-ribosyltransferase 1
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11103
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Expression Region
Lys661~Pro881
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Molecular Weight
29kDa
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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
PARP1 (Poly(ADP-ribose) polymerase 1) is an enzyme that plays a critical role in cellular processes, including DNA repair, genomic stability, and programmed cell death. Research into PARP1 has gained significant momentum due to its involvement in various diseases, particularly cancer. Dysregulation of PARP1 activity is linked to tumorigenesis, making it a promising target for therapeutic intervention. Inhibitors of PARP1 have emerged as a novel class of anti-cancer drugs, especially in treating BRCA1/2-mutated cancers, where they exploit the concept of synthetic lethality. Additionally, PARP1's role in the cellular response to oxidative stress and inflammation further emphasizes its importance in both normal physiology and disease states. Understanding the structure-function relationship of PARP1 through recombinant protein studies allows for insights into its enzymatic activity and regulatory mechanisms, facilitating the development of more effective PARP inhibitors and therapeutic strategies. The ongoing research into PARP1 and its pathways underscores its significance in cancer biology and the potential for targeted treatments that leverage its mechanisms for improved patient outcomes.
