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OTUB1 Antibody (C-Term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q96FW1 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 31284 Da |
| Gene ID | 55611 |
|---|---|
| Other Names | Ubiquitin thioesterase OTUB1, Deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Otubain-1, hOTU1, Ubiquitin-specific-processing protease OTUB1, OTUB1, OTB1, OTU1 |
| Target/Specificity | This OTUB1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 185-219 amino acids from human OTUB1. |
| Dilution | WB~~1:1000-1:2000 |
| 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 | OTUB1 Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | OTUB1 |
|---|---|
| Synonyms | OTB1, OTU1 |
| Function | Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation (PubMed:12704427, PubMed:14661020, PubMed:12401499, PubMed:23827681). Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen (PubMed:14661020). Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy (PubMed:14661020). Isoform 1 destabilizes RNF128, leading to prevent anergy (PubMed:14661020). In contrast, isoform 2 stabilizes RNF128 and promotes anergy (PubMed:14661020). Surprisingly, it regulates RNF128- mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 (PubMed:14661020). Deubiquitinates estrogen receptor alpha (ESR1) (PubMed:19383985). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (PubMed:19211026, PubMed:23827681, PubMed:18954305). Not able to cleave di-ubiquitin (PubMed:23827681, PubMed:18954305). Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (PubMed:23827681, PubMed:18954305). |
| Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:B2RYG6}. |
| Tissue Location | Isoform 1 is ubiquitous. Isoform 2 is expressed only in lymphoid tissues such as tonsils, lymph nodes and spleen, as well as peripheral blood mononuclear cells |
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Provided below are standard protocols that you may find useful for product applications.
Background
Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys- 48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.
References
Balakirev M.Y.,et al.EMBO Rep. 4:517-522(2003).
Soares L.,et al.Nat. Immunol. 5:45-54(2004).
Zhang Q.-H.,et al.Genome Res. 10:1546-1560(2000).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Taylor T.D.,et al.Nature 440:497-500(2006).
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