Recombinant Human OTUB1 Protein, His-tagged
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|Product Overview :||Recombinant human OTUB1 protein contains an N-terminal 6-His tag was expressed in E.coli.|
|Description :||The product of this gene is a member of the OTU (ovarian tumor) superfamily of predicted cysteine proteases. The encoded protein is a highly specific ubiquitin iso-peptidase, and cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. It interacts with another ubiquitin protease and an E3 ubiquitin ligase that inhibits cytokine gene transcription in the immune system. It is proposed to function in specific ubiquitin-dependent pathways, possibly by providing an editing function for polyubiquitin chain growth. Alternative splicing results in multiple transcript variants.|
|Source :||E. coli|
|Bio-activity :||Recombinant Human His6-Otubain-1 is a Ubiquitin-specific deconjugating enzyme. Reaction conditions will need to be optimized for each specific application. We recommend an initial His6-Otubain-1 concentration of 1-5 μM.|
|Molecular Mass :||32 kDa|
|Purity :||> 95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.|
|Storage :||Avoid repeated freeze-thaw cycles.
12 months from date of receipt, -70 centigrade as supplied.
3 months, -70 centigrade under sterile conditions after opening.
|Storage Buffer :||X mg/ml (X μM) in 50 mM HEPES pH 7.5, 100 mM NaCl, 1 mM TCEP|
|Gene Name :||OTUB1 OTU deubiquitinase, ubiquitin aldehyde binding 1 [ Homo sapiens (human) ]|
|Official Symbol :||OTUB1|
|Synonyms :||OTUB1; OTU deubiquitinase, ubiquitin aldehyde binding 1; OTB1; OTU1; HSPC263; ubiquitin thioesterase OTUB1; OTU domain, ubiquitin aldehyde binding 1; OTU domain-containing ubiquitin aldehyde-binding protein 1; OTU-domain Ubal-binding 1; deubiquitinating enzyme OTUB1; otubain-1; ubiquitin-specific protease otubain 1; ubiquitin-specific-processing protease OTUB1; EC 220.127.116.11|
|Gene ID :||55611|
|mRNA Refseq :||NM_017670|
|Protein Refseq :||NP_060140|
|UniProt ID :||Q96FW1|
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