Analytical Data
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Gene name
PARP2
- Application
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Alternative Names
Poly [ADP-ribose] polymerase 2; ADP-ribosyltransferase diphtheria toxin-like 2; DNA ADP-ribosyltransferase PARP2; NAD(+) ADP-ribosyltransferase 2; ADPRT-2; pADPRT-2; EC:2.4.2.30; ADPRT2; ADPRTL2
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Species
Human
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Source
Baculovirus
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UGN5
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Expression Region
M1-W583
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Protein Length
Full Length
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Molecular Weight
71.6 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
PARP2 (Poly(ADP-ribose) polymerase 2) is a member of the PARP family of enzymes, which play a crucial role in cellular responses to DNA damage and stress, particularly through the post-translational modification of proteins via poly(ADP-ribosyl)ation. Unlike its closely related counterpart PARP1, PARP2 exhibits distinct functions and regulatory mechanisms that contribute to genomic stability and cellular survival. The study of PARP2 has gained significant attention due to its implications in cancer biology; aberrations in its expression or activity can affect tumor progression and response to therapies. Additionally, PARP2 is implicated in various physiological processes, including DNA repair, regulation of gene expression, and modulation of apoptosis. Given the therapeutic potential of targeting PARP enzymes in cancer treatment, the development of detailed structural and functional insights into PARP2 is paramount. Recombinant protein studies of PARP2 allow researchers to elucidate its enzymatic activity, interaction with DNA, and role in the PARP pathway, thus providing valuable information for potential drug development and understanding its contribution to disease mechanisms. These investigations enhance our understanding of PARP2's biological functions and pave the way for novel therapeutic strategies that exploit its activities in cancer and other diseases characterized by DNA repair deficiencies.











