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The protein encoded by DPP7 is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes.
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human DPP7 structures reveal the molecular basis of specific inhibition and the architectural diversity of proline-specific peptidases
The constitutive expression of dipeptidyl peptidase II mRNA in chronic lymphocytic leukemia was demonstrated.
DPP II plays a minor role in the progression of malignant melanocytic lesions
DPP2 is essential for maintaining lymphocytes and fibroblasts in G(0), and its inhibition results in apoptosis mediated by induction of c-Myc (show MYC Antibodies) and p53 (show TP53 Antibodies).
gene deficiency results in Th17 differentiation and peripheral T cells hyperactivation upon TCR stimulation
Data show that an increase in food intake in DPP2 kd mice, which was associated with a significant increase in adipose tissue mass and enhanced liver steatosis but no difference in body weight.
KLF2 (show KLF2 Antibodies) and TOB1 activate the mouse Dpp2 promoter.
Data demonstrate that dipeptidyl peptidase II can form a complex with adenosine deaminase (show ADA Antibodies), but with one order of magnitude higher dissociation constant than that of DPPIV (show DPP4 Antibodies).
The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.
, dipeptidyl aminopeptidase II
, dipeptidyl arylamidase II
, dipeptidyl peptidase 2
, dipeptidyl peptidase II
, dipeptidyl-peptidase II
, quiescent cell proline dipeptidase
, dipeptidyl-peptidase 2
, dipeptidyl-peptidase 7
, dipeptidyl peptidase 7