OTUB2 Protein (His Tag)

OTU domain, ubiquitin aldehyde binding 2 Protein Datasheet

OTUB2 Protein 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.
• Source: Human
• Expression Host: E. Coli

OTUB2 Protein 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
• Molecular 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, pH7.5
  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.
• SDS-PAGE: OTUB2 protein

OTUB2 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. 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.

OTUB2 Protein Description

Ubiquitylation process can be reversed and regulated by a group of proteases called deubiquitylating enzymes (DUBs). Otubains are a family of DUBs that belong to the ovarian tumour (OTU) superfamily of proteins. Otubain 2(OTUB2) is a member of the cysteine protease superfamily 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. The active site is formed at the interface of α3 and the loop connecting strands 4 and 5 of the β-sheet, and contains the catalytic triad, Cys 51, His 224 and Asn 226. The 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. Like other DUBs, otubain 2(OTUB2) cleaves proteins precisely at the ubiquitin-protein bond.

References

1. Balakirev MY. et al., 2003, EMBO Rep. 4 (5): 517–22.
2. Nanao MH. 2004, EMBO reports. 5: 783-8.