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Recombinant Human Dipeptidyl peptidase 9 (DPP9), Truncated

ACP15645

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP15645 Target NameDPP9
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Protein LengthPartialPurity>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 IDQ86TI2
Background Information
  • Uniprot Id

    Q86TI2

  • Target Species

    Human

  • Target Name

    DPP9

  • Target Full Name

    Dipeptidyl peptidase 9

  • Target Function

    Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as an inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis: inhibits pyroptosis by preventing activation of NLRP1 and CARD8 via an unknown mechanism.

  • Target Subcellular Location

    [Isoform 1]: Cytoplasm, cytosol.; [Isoform 2]: Nucleus.

  • Target Protein Families

    Peptidase S9B family, DPPIV subfamily

  • Target Tissue Specificity

    Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain.

  • Target Research Area

    Metabolism

  • Target Synonyms

    Dipeptidyl peptidase 9; Dipeptidyl peptidase IV related protein 2; Dipeptidyl peptidase IV-related protein 2; Dipeptidyl peptidase IX; Dipeptidyl peptidase like protein 9; Dipeptidyl peptidase-like protein 9; Dipeptidylpeptidase 9; Dipeptidylpeptidase IX; DKFZp762F117; DP 9; DP9; DPLP 9; DPLP9; DPP 9; DPP IX; DPP9; DPP9_HUMAN; DPRP 2; DPRP-2; DPRP2; FLJ16073

  • Target Background

    This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. The protein has been shown to have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Although the activity of this protein is similar to that of dipeptidyl peptidase 4 (DPP4), it does not appear to be membrane bound. In general, dipeptidyl peptidases appear to be involved in the regulation of the activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. Several transcript variants of this gene have been described but not fully characterized.

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