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DPP7 / DPPII / DPP2 Antibody, Mouse MAb

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    Human DPP7/DPPII/DPP2 Antibody Product Information
    Immunogen:Human cell-derived DPPII protein (Catalog#10748-H08H)
    Clone ID:2G1C10A9
    Ig Type:Mouse IgG1
    Concentration:
    Endotoxin:
    Formulation:0.2 μm filtered solution in PBS with 5% trehalose
    Preparation:This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human DPPII / DPP7 (rhDPPII; Catalog#10748-H08H; NP_037511.2; Met 1-Leu 492). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
    Other DPP7/DPPII/DPP2 Antibody Products
    DPP7 / DPPII / DPP2 Background

    DPP7 (dipeptidylpeptidase 7), also known as DPPII and DPP2, is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. Dipeptidyl peptidases (DPPs) have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. It localizes to lysosomes. DPP7 localizes to lysosomes and exists as a homodimer via its leucine zipper motif and is involved in the degradation of oligopeptides. In response to calcium release, it can be secreted in its active form. It is essential for lymphocyte survival, as the inhibition of DPP7 results in quiescent cell apoptosis.

    Human DPP7 / DPPII / DPP2 References
  • Chiravuri M, et al. (1999) A novel apoptotic pathway in quiescent lymphocytes identified by inhibition of a post-proline cleaving aminodipeptidase: a candidate target protease, quiescent cell proline dipeptidase. J Immunol. 163(6):3092-9.
  • Fukasawa KM, et al. (2001) Cloning and functional expression of rat kidney dipeptidyl peptidase II. Biochem J. 353(Pt 2):283-90.
  • Fornas E, et al. (1992) Effect of cholesterol and its autooxidation derivatives on endocytosis and dipeptidyl peptidases of aortic endothelial cells. Histol Histopathol. 7(2):163-8.
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    Catalog: 10748-MM03-50
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    Datasheet & Documentation

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