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19-205 | Ubiquitin Aldehyde Inhibitor

50 µg  
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      Replacement Information
      Catalogue Number19-205
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionUbiquitin Aldehyde Inhibitor
      Product Information
      Key Applications
      • Inhibits Activity/Function
      Application NotesPurified bovine ubiquitin (Ub) synthetically modified to convert the C-terminal glycine carboxyl to an aldehyde. Potent and specific inhibitor of ubiquitin C-terminal hydrolases (UCHs). Recommended concentration for maximal inhibition is 2-5 µM. Soluble in DMSO and acetonitrile
      Biological Information
      Entrez Gene Number
      Entrez Gene SummaryThis gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to histone H2A in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein has been noticed in patients with Alzheimer's and Down syndrome.
      Gene Symbol
      • RPS27A
      • CEP80
      • ubiquitin
      • ubiquitin-CEP80
      • UBCEP1
      • Ubiquitin.
      • UBA52
      • UBCEP2
      • UBA80
      • UBC
      • UBB
      • HUBCEP80
      Protein TargetRPS27A
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P62988 # Protein modifier which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Attachment to proteins as a Lys-48-linked polymer usually leads to their degradation by proteasome. Attachment to proteins as a monomer or as an alternatively linked polymer does not lead to proteasomal degradation and may be required for numerous fonctions, including maintenance of chromatin structure, regulation of gene expression, stress response, ribosome biogenesis and DNA repair.
      SIZE: 76 amino acids; 8565 Da
      SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
      PTM: Several types of polymeric chains can be formed, depending on the lysine used for the assembly.
      SIMILARITY: SwissProt: P62988 ## Belongs to the ubiquitin family.
      MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains. In some species there is a final amino-acid after the last repeat, here in human a Val. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27a).
      Molecular Weight491.44
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStore at -20°C for up to 1 year. Store solutions at -20°C for up to 3 months.
      Packaging Information
      Material Size50 µg
      Transport Information
      Supplemental Information


      Certificates of Analysis

      TitleLot Number
      Ubiquitin Aldehyde Inhibitor - 0611045518 0611045518


      Reference overviewPub Med ID
      Kinetic studies on the inhibition of isopeptidase T by ubiquitin aldehyde.
      Melandri, F, et al.
      Biochemistry, 35: 12893-900 (1996) 1996

      Show Abstract
      8841133 8841133
      Recognition of modified forms of ribonuclease A by the ubiquitin system
      Dunten, R L and Cohen, R E
      J Biol Chem, 264:16739-16747 (1989) 1989

      2550456 2550456


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