Recombinant Human PARP2 Protein, N-His (PX-P5875) expressed in E. coli, Purity: >90% as determined by SDS-PAGE..
Highlights
High Purity (>90% as determined by SDS-PAGE.) — Verified by SDS-PAGE for downstream accuracy.
E. coli Expression — Optimized for functional studies.
表达系统
E. coli
Accession号
Q9UGN5
蛋白长度
Ser223-Trp583
应用
ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
种属
Homo sapiens (Human)
性质
Recombinant
内毒素水平
Please contact with the lab for this information.
纯度
>90% as determined by SDS-PAGE.
预测分子量
43.20 kDa
状态
Lyophilized
保存溶液
Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
重悬
Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
运输
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
稳定性和存储
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Poly [ADP-ribose] polymerase 2 (PARP2) is a ~66 kDa protein. Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site.
1. Amé, JC. et al. (1999) The Journal of biological chemistry 274, 17860-8. PMID: 10364231
2. Vyas, S. et al. (2014) Nature communications 5, 4426. PMID: 25043379
3. Talhaoui, I. et al. (2016) Nucleic acids research 44, 9279-9295. PMID: 27471034
