Recombinant Human Ubiquitin Thioesterase Otub1 (OTUB1) Protein (GST)

Name: Recombinant Human Ubiquitin Thioesterase Otub1 (OTUB1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03608P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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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	HGNC: 23077 OMIM: 608337 KEGG: hsa:55611 STRING: 9606.ENSP00000402551 UniGene: 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

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.