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DPP3 encodes a protein that is a member of the M49 family of metallopeptidases.
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We conclude that DPP 3 may influence the cellular expression of Ang-(1 (show ANGPT1 Antibodies)-7) and potentially reflect a therapeutic target to augment the actions of the peptide
biological function of human dipeptidyl peptidase III
several crystal structures of complexes of human dipeptidyl peptidase III with different peptides.
the DPP III conformational landscape and the influence of ligand binding on the protein structure and dynamics, was investigated.
The study used three different conformations of human dipeptidyl-peptidase III (DPP III) to investigate the influence of the protein environment on ligand binding and the Zn(2+) coordination.
Deletion/mutagenesis of C/EBP-beta (show CEBPB Antibodies) binding motif of DPP III promoter significantly increased its activity and abolished its responsiveness to IL-6 (show IL6 Antibodies) in glioblastoma cells.
The activity of the yeast and human dipeptidyl peptidase III were examined.
Combined results of mutational analysis and mass spectrometry suggest that glutathionylation (formation of mixed disulfide) of Cys176 and Cys654 contributes to human DPP III inactivation by oxidized glutathione.
Amplification and mRNA overexpression of the DPP3 gene is associated with squamous cell lung carcinomas.
results provide the basis for the design of specific inhibitors that enable the elucidation of the exact role of DPP III and the exploration of its potential as a target of pain intervention strategies
the cellular peptidases dipeptidyl peptidase 3 (DPP-3) and thimet oligopeptidase 1 (show THOP1 Antibodies) (TOP-1 (show TOP1 Antibodies)), both of which are present in nonimmunogenic necrotic cells, eliminated proteasomal degradation products and blocked Ag cross-presentation
This gene encodes a protein that is a member of the M49 family of metallopeptidases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternatively spliced transcript variants have been found for this gene.
, dipeptidyl aminopeptidase III
, dipeptidyl arylamidase III
, dipeptidyl peptidase 3
, dipeptidyl peptidase III
, dipeptidyl-peptidase 3
, dipeptidyl-peptidase III
, dipeptidylpeptidase III
, dipeptidylpeptidase 3
, Dipeptidyl-peptidase 3
, Dipeptidyl-peptidase III
, dipeptidyl aminopeptidase
, LOW QUALITY PROTEIN: dipeptidyl peptidase 3