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DPP9 encodes a protein that is a member of the S9B family in clan SC of the serine proteases. Additionally we are shipping DPP9 Antibodies (78) and DPP9 Proteins (5) and many more products for this protein.
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The data of this study have shown that fibroblasts and keratinocytes of normal skin endogenously express DPP9 both at transcriptional and protein level. It is localized intracellularly, mostly in cytoplasm, whereby the sub-localization within Golgi is very scarce.
Liver PFK1 isoform assembles into filaments in a tetramer- and substrate-dependent manner,organizing isoform specific glucose metabolism in cells.
DPP9 has a role in promoting tumorgenicity, metastasis and the prediction of poor prognosis in non-small cell lung cancer
The DPP9 expressing cell model system is a very useful and promising system for investigating the selectivity and associated toxicity of DPP4 (show DPP4 ELISA Kits) inhibitors on DPP9.
There was a concomitant decrease in the phosphorylation of focal adhesion kinase and paxillin (show PXN ELISA Kits), indicating that DPP9 knockdown or enzyme inhibition suppressed the associated adhesion signaling pathway, causing impaired cell movement.
Whereas DPP9-short is present in the cytosol, DPP9-long localizes preferentially to the nucleus.
The SUMO1 (show SUMO1 ELISA Kits)-E67 interacting loop peptide is an allosteric inhibitor of the dipeptidyl peptidases 8 and 9.
Suggest roles for DPP8 (show DPP8 ELISA Kits) and DPP9 in lymphocyte activation and apoptosis and in hepatocytes during liver disease pathogenesis.
DPP9 was found in macrophages of carotid atherosclerotic plaque and may play a role in disease progression.
DPP9 binds to SUMO1 (show SUMO1 ELISA Kits) through a novel SUMO1 (show SUMO1 ELISA Kits) interacting motif.
lack of DPP9 activity in mice leads to impaired tongue development, suckling defect and subsequent neonatal lethality.
Changes induced by DPP9 gene silencing in macrophages suggest possible role of DPP9 in regulation of proliferation and activation status, as well as in peptide processing within endosomal/vesicular compartment.
DPP9 enzyme activity regulates metabolic pathways in neonatal liver and gut (show GUSB ELISA Kits).
Blocking the expression or activities of DPP8 (show DPP8 ELISA Kits) and DPP9 attenuates PPARgamma2 (show PPARG ELISA Kits) induction during preadipocyte differentiation.
Identification of novel dipeptidyl peptidase 9 substrates: discovering dipeptide Val-Ala as a consensus site for DPP9 cleavage
DPP9 enzymatic activity is essential for early neonatal survival in mice.
DP8 (show DPP8 ELISA Kits) and DP9 tissue and cellular expression
Properties of DPP9 are reported, including functional stability and sensitivity towards metal ions. The short form of DPP9 can be isolated from testes and it behaves as a stable enzyme.
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.
6-phosphofructokinase, liver type
, liver-type 1-phosphofructokinase
, phosphofructo-1-kinase isozyme B
, phosphofructokinase 1
, DPP IX
, dipeptidyl peptidase 9
, dipeptidyl peptidase IV-related protein 2
, dipeptidyl peptidase IV-related protein-2
, dipeptidyl peptidase IX
, dipeptidyl peptidase-like protein 9
, dipeptidylpeptidase 9
, dipeptidyl-peptidase 9