Recombinant Human OTUB2 Protein (Catalog#13177-H07E)
This antibody was obtained from a rabbit immunized with purified, recombinant Human OTUB2 (rh OTUB2; Catalog#13177-H07E; Q96DC9-1; Met1-His234).
Monoclonal Rabbit IgG Clone #139
0.2 μm filtered solution in PBS
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Immunofluorescence staining of Human OTUB2 in A549 cells. Cells were fixed with 4% PFA, permeabilzed with 0.3% Triton X-100 in PBS, blocked with 10% serum, and incubated with rabbit anti-Human OTUB2 monoclonal antibody (1:60) at 4℃ overnight. Then cells were stained with the Alexa Fluor® 549-conjugated Goat Anti-rabbit IgG secondary antibody (red). Positive staining was localized to cytoplasm and nucleus.
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.
OTU deubiquitinase, ubiquitin aldehyde binding 2
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.