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- Signalway Antibody
- USA
- AP77339
- 2025年07月13日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
Store at -20˚C
- 英文名：
Recombinant Human E3 SUMO-protein ligase RanBP2(RANBP2),partial
- 库存：
详询
- 供应商：
南京莱富赛
- 规格：
详询
host_species:E.coli
purification:Greater than 90% as determined by SDS-PAGE.
other_names:358KDA nucleoporin Nuclear pore complex protein Nup358 Nucleoporin Nup358 Ran-binding protein 2
accession_no:P49792
calculated_mw:36.8 kDa
tag info:N-terminal 6xHis-B2M-tagged
Immunogen Description:Expression Region:2601-2802aa
Sequence Info:Partial
formulation:Tris-based buffer50% glycerol
storage:The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃,-80℃. The shelf life of lyophilized form is 12 months at -20℃,-80℃.
Notes:Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
background:E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle
产品详细信息请点击：Recombinant Human E3 SUMO-protein ligase RanBP2(RANBP2),partial
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文献和实验Reconstitution of CHIP E3 Ubiquitin Ligase Activity
CHIP, the carboxyl-terminus of Hsp70 interacting protein, is both an E3 ubiquitin ligase and an Hsp70 co-chaperone and is implicated in the degradation of cytosolic quality control and numerous disease substrates. CHIP has been shown
Performing In Vitro Sumoylation Reactions Using Recombinant Enzymes
to perform in vitro sumoylation reactions, namely the E1 activating enzyme Aos1/Uba2 (SAE1/SAE2), the E2 conjugating enzyme Ubc9, SUMO-1 (identical protocols can be used for SUMO-2/3), and the catalytic domain of the E3 ligase RanBP2/Nup358. Two alternative
Purification and Characterization of Legionella U-Box-Type E3 Ubiquitin Ligase
LubX is one such bacterial E3 ubiquitin ligase. We describe here the method to purify soluble LubX protein using GST-tag and Escherichia coli overexpression systems. Using the purified protein together with recombinant ubiquitin, E1, and E2 enzymes
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