- Remove All
- Your shopping cart is currently empty
Otubain 2 (OTUB2) is a member of DUBs that belong to the ovarian tumour (OTU) superfamily of proteins which consists of a five-stranded β-sheet sandwiched in between a small helical amino-terminal region consisting of α1 and α2, and a large helical region comprised of α3-α10. Like other DUBs, otubain 2 (OTUB2) cleaves proteins precisely at the ubiquitin-protein bond so that ubiquitylation process can be reversed and regulated. Otubain 2 (OTUB2)'s active-site cleft is sterically occluded by a novel loop conformation resulting in an oxyanion hole, which consists uniquely of backbone amides. Furthermore, the residues that orient and stabilize the active-site histidine of otubain 2 (OTUB2) are different from other cysteine proteases. This reorganization of the active-site topology provides a possible explanation for the low turnover and substrate specificity of the otubains.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
100 μg | 282 € | 7-10 days |
Biological Activity | Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | Otubain 2 (OTUB2) is a member of DUBs that belong to the ovarian tumour (OTU) superfamily of proteins which consists of a five-stranded β-sheet sandwiched in between a small helical amino-terminal region consisting of α1 and α2, and a large helical region comprised of α3-α10. Like other DUBs, otubain 2 (OTUB2) cleaves proteins precisely at the ubiquitin-protein bond so that ubiquitylation process can be reversed and regulated. Otubain 2 (OTUB2)'s active-site cleft is sterically occluded by a novel loop conformation resulting in an oxyanion hole, which consists uniquely of backbone amides. Furthermore, the residues that orient and stabilize the active-site histidine of otubain 2 (OTUB2) are different from other cysteine proteases. This reorganization of the active-site topology provides a possible explanation for the low turnover and substrate specificity of the otubains. |
Species | Human |
Expression System | E. coli |
Tag | N-His |
Accession Number | Q96DC9-1 |
Synonyms | OTU2,OTU deubiquitinase, ubiquitin aldehyde binding 2,OTB2,C14orf137 |
Construction | A DNA sequence encoding the human OTUB2 (Q96DC9-1) (Met 1-His 234) was expressed, with a polyhistide tag at the N-terminus. Predicted N terminal: Met |
Protein Purity | > 97 % as determined by SDS-PAGE |
Molecular Weight | 29 kDa (predicted); 30 kDa (reducing conditions) |
Endotoxin | Please contact us for more information. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, 10% glycerol, pH 7.5. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage | It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | In general, Lyophilized powders are shipping with blue ice. |
Research Background | Otubain 2 (OTUB2) is a member of DUBs that belong to the ovarian tumour (OTU) superfamily of proteins which consists of a five-stranded β-sheet sandwiched in between a small helical amino-terminal region consisting of α1 and α2, and a large helical region comprised of α3-α10. Like other DUBs, otubain 2 (OTUB2) cleaves proteins precisely at the ubiquitin-protein bond so that ubiquitylation process can be reversed and regulated. Otubain 2 (OTUB2)'s active-site cleft is sterically occluded by a novel loop conformation resulting in an oxyanion hole, which consists uniquely of backbone amides. Furthermore, the residues that orient and stabilize the active-site histidine of otubain 2 (OTUB2) are different from other cysteine proteases. This reorganization of the active-site topology provides a possible explanation for the low turnover and substrate specificity of the otubains. |
Copyright © 2015-2024 TargetMol Chemicals Inc. All Rights Reserved.