Recombinant Human Ubiquitin Thioesterase Otub1 (OTUB1) Protein (GST)
Beta LifeScience
SKU/CAT #: BLC-03608P
Greater than 90% as determined by SDS-PAGE.
Recombinant Human Ubiquitin Thioesterase Otub1 (OTUB1) Protein (GST)
Beta LifeScience
SKU/CAT #: BLC-03608P
Collections: Other recombinant proteins, Recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Ubiquitin Thioesterase Otub1 (OTUB1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | Q96FW1 |
Target Symbol | OTUB1 |
Synonyms | Deubiquitinating enzyme OTUB1; hOTU1; HSPC263; OTB1; OTU domain containing ubiquitin aldehyde binding protein 1; OTU domain, ubiquitin aldehyde binding 1; OTU domain-containing Ubal-binding protein 1; OTU domain-containing ubiquitin aldehyde-binding protein 1; OTU-domain Ubal-binding 1; OTU1; Otub1; OTUB1_HUMAN; Otubain 1; Otubain-1; Ubiquitin specific processing protease OTUB1; Ubiquitin thioesterase OTUB1; ubiquitin-specific protease otubain 1; Ubiquitin-specific-processing protease OTUB1 |
Species | Homo sapiens (Human) |
Expression System | E.coli |
Tag | N-GST |
Target Protein Sequence | AAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVK |
Expression Range | 2-201aa |
Protein Length | Partial |
Mol. Weight | 50.1kDa |
Research Area | Immunology |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target 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. 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.; Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain. |
Subcellular Location | Cytoplasm. |
Protein Families | Peptidase C65 family |
Database References | |
Tissue Specificity | 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. |
Gene Functions References
- Overexpression of OTUB1 (OTU domain-containing ubiquitin aldehyde binding protein 1) in hepatocellular carcinoma (HCC) could be a supplementary biomarker for HCC because it plays a vital role in the progression of HCC. PMID: 28575188
- Silencing of OTU domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) inhibits migration of human glioma cells in vitro. Study results suggested that OTUB1 was a valuable marker in the pathogenesis of human gliomas and could be used as a novel biomarker for glioma therapy in the future. PMID: 28139865
- Data suggest that inhibiting OTUB1-FOXM1 interaction is a potential avenue for ovarian cancer therapy. PMID: 27167337
- Data indicate that knockdown of otubain 1 protein (Otub1) reduced the levels of double minute 4 protein (MDMX). PMID: 28035068
- OTUB1 may play an important role in colon cancer development and metastasis. PMID: 24947413
- An increase of OTUB1 expression is commonly observed in non-small-cell lung carcinomas harboring wild-type KRAS and is associated with increased levels of ERK1/2 phosphorylation, high Ki67 score, and poorer patient survival. PMID: 26881969
- the data suggest that OTUB1 limits the ubiquitination and degradation of FOXM1 in breast cancer and has a key role in genotoxic agent resistance. PMID: 26148240
- substrate for hydroxylation by FIH on N22 PMID: 26752685
- Data show that casein kinase 2 (CK2)-mediated phosphorylation of deubiquitylating enzyme OTUB1 at Ser16 causes nuclear accumulation of OTUB1. PMID: 25872870
- OTUB1 promoted the metastasis of CRC cell lines. PMID: 25431208
- After viral infection, HSCARG interacted with tumor necrosis receptor-associated factor 3 (TRAF3) and inhibited its ubiquitination by promoting the recruitment of OTUB1 to TRAF3. PMID: 24763515
- These data reveal novel insights into the Otub1 inhibition of E2 wherein monoubiquitination promotes the interaction of Otub1 with UbcH5 and the function to suppress it. PMID: 24403071
- OTUB1 enhances TGF-beta signaling by inhibiting the ubiquitylation and degradation of active SMAD2 and SMAD3. PMID: 24071738
- A second role of OTUB1-E2 interactions is to stimulate OTUB1 cleavage of Lys48 polyubiquitin. This stimulation is regulated by the ratio of charged to uncharged E2 and by the concentration of Lys48-linked polyubiquitin and free ubiquitin. PMID: 23955022
- These results suggest that OTUB1 regulates NF-kappaB and MAPK signalling pathways and TNF-dependent cell death by modulating c-IAP1 stability. PMID: 23524849
- the crystal structure of human OTUB1 in complex with human UBC13 and MMS2 PMID: 22679021
- structural and biochemical studies elucidating how OTUB1 inhibits UBC13 and other E2 enzymes PMID: 22367539
- OTUB1 therefore co-opts Lys48-linked ubiquitin chain recognition to suppress ubiquitin conjugation and the DNA damage response PMID: 22325355
- Overexpression of Otub1(D88A) or ablation of endogenous Otub1 by siRNA markedly impaired p53 stabilization and activation in response to DNA damage. Together, these results reveal a novel function for Otub1 in regulating p53 stability and activity PMID: 22124327
- OTUB1, a deubiquitinating enzyme, is an inhibitor of double-strand break-induced chromatin ubiquitination PMID: 20725033
- Post-translational modifications of OTUB1 suggests a new entry point for manipulating Yersinia interactions with the host. PMID: 20553488
- Findings suggest that OTUB1 and OTUB2 negatively regulate virus-triggered type I IFN induction and cellular antiviral response by deubiquitinating TRAF3 and -6. PMID: 19996094
- Structural basis and specificity of human otubain 1-mediated deubiquitination. PMID: 18954305
- Distinct binding sites for the ubiquitins on either side of the scissile bond allow hOtu1 to discriminate among different isopeptide linkages in polyubiquitin substrates. PMID: 19211026
- OTUB1 negatively regulates transcription mediated by ERalpha in transient reporter gene assays and transcription mediated by endogenous ERalpha in Ishikawa endometrial cancer cells PMID: 19383985