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UBE2N Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P61088 |
| Reactivity | Human, Rat |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 17138 Da |
| Gene ID | 7334 |
|---|---|
| Other Names | Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, UbcH13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU |
| Target/Specificity | This UBE2N antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 41-74 amino acids from the Central region of human UBE2N. |
| Dilution | WB~~1:2000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | UBE2N Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | UBE2N |
|---|---|
| Synonyms | BLU |
| Function | The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly- ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'- linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1- UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'- linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UB2V1, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed:28469175, PubMed:31006531). UBE2V1- UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'- linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway. |
| Cellular Location | Nucleus. Cytoplasm |
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Provided below are standard protocols that you may find useful for product applications.
Background
The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity).
References
Yamaguchi T.,et al.J. Biochem. 120:494-497(1996).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Lubec G.,et al.Submitted (DEC-2008) to UniProtKB.
Zou W.,et al.Biochem. Biophys. Res. Commun. 336:61-68(2005).
Hofmann R.M.,et al.Cell 96:645-653(1999).
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