Recombinant human UCHL3 protein (Active)
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Recombinant human UCHL3 protein (Active) is a Human Full Length protein, in the 1 to 230 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, Ubiquitin thioesterase L3, UCHL3
- FuncS
Supplier Data
Functional Studies - Recombinant human UCHL3 protein (Active) (AB269111)
Protein activity of ab269111 was determined to be 29 nmol/min/mg in a DUB assay using ubiquitin-based proluciferin substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human UCHL3 protein (Active) (AB269111)
SDS-PAGE analysis of ab269111.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Ubiquitin carboxyl-terminal hydrolase L3 functions to regulate protein stability and signaling pathways by reversing protein ubiquitination. UCHL3 acts independently but can sometimes associate with complexes involved in cellular stress responses. Deubiquitinase activity makes it a critical regulator that modulates proteins involved in DNA repair transcriptional regulation and cell cycle progression. This regulation has vast implications for cellular growth differentiation and survival.
Pathways
UCHL3 plays significant roles in the ubiquitin-proteasome pathway and the DNA damage response pathway. By participating in these pathways UCHL3 influences cellular pathways that control protein quality control and genomic stability. It interacts with proteins such as p53 and BRCA1 influencing their stability and function. UCHL3's activity affects cellular responses to stress and repair processes thereby maintaining cellular integrity and promoting cancer prevention mechanisms.
Specifications
Form
Liquid
General info
Function
Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3'', and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.
Sequence similarities
Belongs to the peptidase C12 family.
Target data
Product promise
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