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Recombinant Human Ubiquitin carboxyl-terminal hydrolase 1 (USP1)

ACP21042

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP21042 Target NameUSP1
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Expression Range1-785Protein LengthFull length protein
Purity>85% (SDS-PAGE)Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDO94782
Background Information
  • Uniprot Id

    O94782

  • Target Species

    Human

  • Target Name

    USP1

  • Target Full Name

    Ubiquitin carboxyl-terminal hydrolase 1

  • Target Function

    Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity.

  • Target Subcellular Location

    Nucleus.

  • Target Protein Families

    Peptidase C19 family

  • Target Synonyms

    Deubiquitinating enzyme 1; hUBP; Ubiquitin carboxyl terminal hydrolase 1; Ubiquitin carboxyl-terminal hydrolase 1; Ubiquitin specific peptidase 1; Ubiquitin specific protease 1; Ubiquitin thioesterase 1; Ubiquitin thiolesterase 1; Ubiquitin-specific-processing protease 1; UBP; UBP1_HUMAN; USP 1; Usp1

  • Target Background

    This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the cytoplasm and cleaves the ubiquitin moiety from ubiquitin-fused precursors and ubiquitinylated proteins. The protein specifically deubiquitinates a protein in the Fanconi anemia (FA) DNA repair pathway. Alternate transcriptional splice variants have been characterized.

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