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Human OTUB2 Protein (His Tag)

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OTUB2Protein Product Information
Synonym:C14orf137, FLJ21916, MGC3102, OTB2, OTU2
Protein Construction:A DNA sequence encoding the human OTUB2 (Q96DC9-1) (Met 1-His 234) was expressed, with a polyhistide tag at the N-terminus.
Species:Human
Expressed Host:E. coli
Form & Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
OTUB2Protein QC Testing
Purity:> 97 % as determined by SDS-PAGE
Endotoxin:Please contact us for more information.
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Met
Molecule Mass:The recombinant human OTUB2 consisting of 249 amino acids and has a calculated molecular mass of 29 kDa. It migrates as an approximately 30 kDa band in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile PBS, 10% glycerol, pH 7.5
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
OTUB2Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
13177-H07E
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.

References
  • Balakirev MY, et al. (2003) Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep 4 (5): 517-22.
  • Nanao MH. (2004) Crystal structure of human otubain 2. EMBO reports. 5: 783-8.
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    Catalog:13177-H07E-50
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    • Human OTUB2 Protein (His Tag) SDS-PAGE
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