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  • 产品名称：Ubiquitin-ConjugatingEnzymeE2F(Putative)(UBE2F)(AA1-185)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
Ubiquitin-ConjugatingEnzymeE2F(Putative)(UBE2F)(AA1-185)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 21.9 kDa. The protein migrates as 23-25 kDa under reducing (R) condition (SDS-PAGE).
Purity >90 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background Ubiquitin-conjugating enzyme E2 F (UBE2F), a member of the ubiquitin-conjugating enzyme family and UBE2F subfamily, is also known as NEDD8-conjugating enzyme UBE2F, NEDD8 carrier protein UBE2F and NEDD8-conjugating enzyme 2 (NCE2),which can interact with UBA3 and RBX2. The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins.UBE2F also can accept the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyze its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.
Molecular Weight 21.9 kDa
UniProt Q969M7
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Ubiquitin-Conjugating Enzyme E2F (Putative) (UBE2F) (AA 1-185) (Active) protein (His tag) (ABIN2181885) Human UBE2F, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ov...
Background publications Monda, Scott, Miller, Lydeard, King, Harper, Bennett, Schulman: "Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes." in: Structure (London, England : 1993), Vol. 21, Issue 1, pp. 42-53, 2013 (PubMed).

Huang, Ayrault, Hunt, Taherbhoy, Duda, Scott, Borg, Neale, Murray, Roussel, Schulman: "E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification." in: Molecular cell, Vol. 33, Issue 4, pp. 483-95, 2009 (PubMed).