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應用
DPP9 is a protease of the DPP4 gene family that is used in cancer research to study the regulation of survival and proliferation pathways. DPP9 is used to study cell-extracellular matrix interactions and tissue remodeling.
生化／生理作用
DPP IX is a member of the S9b family of dipeptidyl peptidases and cleaves the peptide hormones glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide Y and peptide YY with marked kinetic differences compared with dipeptidyl peptidase IV. It has a role in regulating cell survival and proliferation through modulating molecular signaling cascades. Protein kinase B activation is significantly inhibited by human DPP9 overexpression in human hepatoma cells (HepG2 and Huh7) and human embryonic kidney cells (HEK293T). DPP9 is thought to influence cell-extracellular matrix interactions and may be involved in the regulation of tissue remodeling .
物理性質
Full length sequence with an N-terminal GST tag
單位定義
DPP IX is a member of the S9b family of dipeptidyl peptidases. and cleaves the peptide hormones glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide Y and peptide YY with marked kinetic differences compared with dipeptidyl peptidase IV.
One unit will hydrolyze 1.0 picomole of H-Gly-Pro-AMC per minute at pH 7.5 at 25 deg °C
外觀
Supplied as a solution in 40 mM Tris-HCl pH 8.0, 110 mM NaCl, 2.2 mM KCl, 20% glycerol, 3 mM DTT, and 16 mM glutathione
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 1
Denise M T Yu et al.
The FEBS journal, 273(11), 2447-2460 (2006-05-18)
The dipeptidyl peptidase IV gene family contains the four peptidases dipeptidyl peptidase IV, fibroblast activation protein, dipeptidyl peptidase 8 and dipeptidyl peptidase 9. Dipeptidyl peptidase IV and fibroblast activation protein are involved in cell-extracellular matrix interactions and tissue remodeling. Fibroblast
Tsun-Wen Yao et al.
Molecular cancer research : MCR, 9(7), 948-959 (2011-05-31)
Dipeptidyl peptidase IV (DPP4), DPP8, DPP9, and fibroblast activation protein (FAP), the four proteases of the DPP4 gene family, have unique peptidase and extra-enzymatic activities that have been implicated in various diseases including cancers. We report here a novel role
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