Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP15374
    • SpeciesHuman
    • SequenceMGSSHHHHHHSSGLVPRGSHMEGQRWLPLEANPEVTNQFLKQLGLHPNWQ FVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDV TSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMS PEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHL YELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
    • Molecular weight28 kDa including tags
    • Amino acids1 to 230
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab103502 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activitySpecific activity: >3,000 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at pH 8.0, at 37°C.
    Activity Assay:
    1. Prepare a 100ul of recombinant UCH-L3 protein with various concentrations (0.48ng, 0.9ng) in assay buffer and equilibrate to 37°C for 10 minutes. (Assay buffer: 50mM Tris-HCl, 0.5 mM EDTA, 1 mM DTT, 0.1 mg/ml Ovalbumin, pH 8.0.)
    2. Add 50ul of 1uM Ubiquitin-AMC.
    3. Read at excitation wavelengths 355nm and emission 460nm for 5 minutes.
      - Ubiquitin-AMC
      - 96 Well Polystyrene Microplate, black
      - Fluorescent plate reader (PerkinElmer, VICTOR X3)
  • Applications

    Functional Studies

    SDS-PAGE

  • Mass spectrometry
    MALDI-TOF
  • Purity> 95 % SDS-PAGE.
    ab103502 purified by using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.
  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 10% Glycerol, 20mM Tris HCl, 1mM DTT, pH 8.0

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • Ubiquitin carboxyl-terminal hydrolase isozyme L3
    • Ubiquitin thioesterase L3
    • Ubiquitin thiolesterase
    • Ubiquitin thiolesterase L3
    • UCH L3
    • UCH-L3
    • UCHL3
    • UCHL3_HUMAN
    see all
  • FunctionDeubiquitinating 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". 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.
  • Tissue specificityHighly expressed in heart, skeletal muscle, and testis.
  • Sequence similaritiesBelongs to the peptidase C12 family.
  • Post-translational
    modifications
    Phosphorylated upon DNA damage, probably by ATM or ATR.
  • Cellular localizationCytoplasm.
  • Information by UniProt

Recombinant human UCHL3 protein images

  • 15% SDS-PAGE analysis of 3µg ab103502.

References for Recombinant human UCHL3 protein (ab103502)

ab103502 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"