Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
DPP9 encodes a protein that is a member of the S9B family in clan SC of the serine proteases. De plus, nous expédions DPP9 Kits (12) et DPP9 Protéines (6) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 96 products:
Human Monoclonal DPP9 Primary Antibody pour FACS, IF - ABIN2719729
Zhang, Chen, Wadham, McCaughan, Keane, Gorrell: Dipeptidyl peptidase 9 subcellular localization and a role in cell adhesion involving focal adhesion kinase and paxillin. dans Biochimica et biophysica acta 2015
Human Monoclonal DPP9 Primary Antibody pour WB - ABIN2719737
Huan, Jiang, Liu, Shen: Establishment of a dipeptidyl peptidases (DPP) 8/9 expressing cell model for evaluating the selectivity of DPP4 inhibitors. dans Journal of pharmacological and toxicological methods 2015
we found a DPP9-PPP6R3 (Montrer PPP6R3 Anticorps) fusion transcript in one tumor showing a matching genomic 11;19-translocation. Another tumor had a rearrangement of DPP9 with PLIN3 (Montrer PLIN3 Anticorps). Both rearrangements were associated with diminished expression of the 3' end of DPP9 corresponding to the breakpoints identified by RNA-seq.
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.
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 (Montrer DPP4 Anticorps) inhibitors on DPP9.
There was a concomitant decrease in the phosphorylation of focal adhesion kinase and paxillin (Montrer PXN Anticorps), 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 (Montrer SUMO1 Anticorps)-E67 interacting loop peptide is an allosteric inhibitor of the dipeptidyl peptidases 8 and 9.
Suggest roles for DPP8 (Montrer DPP8 Anticorps) 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 (Montrer SUMO1 Anticorps) through a novel SUMO1 (Montrer SUMO1 Anticorps) 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 (Montrer GUSB Anticorps).
Blocking the expression or activities of DPP8 (Montrer DPP8 Anticorps) and DPP9 attenuates PPARgamma2 (Montrer PPARG Anticorps) 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 (Montrer DPP8 Anticorps) 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.
, 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