Background：Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3), a member of peptidase C12 family, is also known as ubiquitin thioesterase L3.
Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins.
UCH-L3 is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8.
UCH-L3 indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis.
It is also required for stress-response retinal, skeletal muscle and germ cell maintenance.
Furthermore, UCH-L3 may be involved in working memory and can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.
仕様
サイズ：100ug
Source：Human UCH-L3, His Tag (UC3-H5141) is expressed from E.coli cells. It contains AA Glu 2 - Ala 230 (Accession # P15374-1).
Molecule：UCH-L3
Synonyms：UCHL3,Ubiquitin thioesterase L3
Species：Human
Tag：His Tag
Expression Systems：E.coli
Expression Rigeion：Glu 2 - Ala 230
Conjugate：Unconjugated
Accession：AAH18125.1
Molecular Weight：27.0 kDa
Characteristics：This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 27.0 kDa. The protein migrates as 27 kDa under reducing (R) condition (SDS-PAGE).
Endotoxin Level：Less than 1.0 EU per ug by the LAL method.
