ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Species
Homo sapiens (Human)
Nature
Recombinant
Endotoxin level
Please contact with the lab for this information.
Purity
>90% as determined by SDS-PAGE.
Predicted molecular weight
34.15 kDa
Form
Lyophilized
Storage buffer
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Reconstitution
Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage
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.
Alternate Names
DDXBP1, DEAD/H box-binding protein 1, E3 SUMO-protein ligase PIAS1, E3 SUMO-protein transferase PIAS1, EC:2.3.2.-, GBP, Gu-binding protein, PIAS1, Protein inhibitor of activated STAT protein 1, RNA helicase II-binding protein
Background
E3 SUMO-protein ligase PIAS1 is a ~71 kDa protein. Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2, PML and ZNF76. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context.
1. Kahyo, T. et al. (2001) Molecular cell 8, 713-8. PMID: 11583632
2. Schmidt, D. et al. (2002) Proceedings of the National Academy of Sciences of the United States of America 99, 2872-7. PMID: 11867732
3. Kadaré, G. et al. (2003) The Journal of biological chemistry 278, 47434-40. PMID: 14500712
4. Zheng, G. et al. (2004) The Journal of biological chemistry 279, 42410-21. PMID: 15280358
5. Cong, L. et al. (2011) The Journal of biological chemistry 286, 43793-43808. PMID: 21965678
6. Zhang, T. et al. (2022) Nature communications 13, 5133. PMID: 36050397
中文
English
한국어
日本語
Español
Français
Русский
