Analytical Data
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Gene name
PARP11
- Application
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Alternative Names
ADP-ribosyltransferase diphtheria toxin-like 1 ;ARTD1NAD(+) ADP-ribosyltransferase 1 ;ADPRT 1;Poly[ADP-ribose] synthase 1
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Species
Human
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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
Q9NR21
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Expression Region
9-338aa
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Molecular Weight
41 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
PARP11 (Poly(ADP-ribose) polymerase 11) is a member of the PARP family of enzymes known for their role in the cellular response to DNA damage and regulation of various biological processes through ADP-ribosylation. Research on PARP11 has gained momentum due to its involvement in cellular stress responses, cancer biology, and potential therapeutic applications. Unlike its better-characterized relatives, PARP1 and PARP2, PARP11 exhibits unique regulatory roles and can influence various signaling pathways, particularly those related to RNA metabolism and immune responses. Recent studies suggest that PARP11 may modulate the stability and translation of specific mRNAs, highlighting its significance in post-transcriptional regulation. Moreover, abnormal expression or mutations in PARP11 have been associated with various malignancies, making it a potential biomarker for cancer progression and a target for novel therapeutic strategies. Investigating the structure and function of the PARP11 recombinant protein can provide deeper insights into its enzymatic mechanisms and interactions with substrates, paving the way for innovative treatments that could exploit its unique properties in cancer therapy and other diseases linked with dysregulated PARP activity. As such, ongoing research into PARP11 not only enhances our understanding of PARP family enzymes but also opens avenues for targeted interventions in conditions where PARP11 plays a crucial role.
