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Your Position: Home > Enzymes > Human UCH-L3 / UCHL3 Protein

Human UCH-L3 / UCHL3 Protein

  • Synonym
    UCHL3,Ubiquitin thioesterase L3
  • Source
    Human UCH-L3, His Tag (UC3-H5141) is expressed from E.coli cells. It contains AA Glu 2 - Ala 230 (Accession # AAH18125).
    Predicted N-terminus: Met
  • Molecular Characterization
    UCH-L3(Glu 2 - Ala 230) AAH18125

    This protein carries a polyhistidine tag at the N-terminus.

    The protein has a calculated MW of 27 kDa. The protein migrates as 27 kDa under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    No activity loss is observed after storage at:

    1. 4-8°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Human UCH-L3, His Tag (Cat. No. UC3-H5141) SDS-PAGE gel

Human UCH-L3, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

  • 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.
  • References
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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