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OTUB2 Protein, Human, Recombinant (His)

Catalog No. TMPY-02522
Synonyms: OTU deubiquitinase, ubiquitin aldehyde binding 2, OTU2, OTB2, C14orf137

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.

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OTUB2 Protein, Human, Recombinant (His)
Pack Size Availability Price/USD Quantity
100 μg 5 days $ 297.00
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Biological Description
Technical Params
Product Properties
References and Literature
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 His
Accession Number Q96DC9-1
Synonyms OTU deubiquitinase, ubiquitin aldehyde binding 2, OTU2, 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.
Protein Purity > 97 % as determined by SDS-PAGE
Molecular Weight 29 kDa (predicted)
Endotoxin Please contact us for more information.
Formulation Lyophilized from sterile PBS, 10% glycerol, pH 7.5. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage

Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. 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.

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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.

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.

References and Literature

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Keywords

OTUB2 Protein, Human, Recombinant (His) OTU deubiquitinase, ubiquitin aldehyde binding 2 OTU2 OTU-2 OTB2 C14orf137 OTB 2 OTU 2 OTB-2 recombinant recombinant-proteins proteins protein

 

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