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Human DPP4 Protein expressed in Insect Cells - ABIN5570005
Shiobara, Chibana, Watanabe, Arai, Horigane, Nakamura, Hayashi, Shimizu, Takemasa, Ishii: Dipeptidyl peptidase-4 is highly expressed in bronchial epithelial cells of untreated asthma and it increases cell proliferation along with fibronectin production in airway constitutive cells. in Respiratory research 2016
DPP4 inhibitors have been demonstrated to be beneficial in the improvement of endothelial homeostasis.
As for 18Lin(-), CD34 (show CD34 Proteins)(-) HSCs are characterized by low expression of the tetraspanin CD9, which promotes homing, and high expression of the peptidase CD26, which inhibits homing.
suggests that DPP4 T-molecules have modified binding and functions compared with their FL counterparts and may serve regulatory roles in normal and malignant hematopoiesis
Analysis of both the structures and inhibitory activities suggests that the binding of the trifluorophenyl moiety in the S1 pocket and the piperazine-2-one moiety have hydrophobic interactions with Phe357 in the S2 extensive subsite, and that the multiple hydrogen bonds made by the (R)-beta-amine group in the S2 pocket and the contacts made by the (R)-tert (show TERT Proteins)-butyl group with Arg125 contribute to the high potency observed...
the selective expression of DPP4 on the surface of senescent cells enables their preferential elimination.
Study shows that increased DPP4 activities are independently associated with mild cognitive impairment in elderly patients with type 2 diabetes.
A common variant, i.e., single nucleotide polymorphism rs6741949, in the DPP4 gene interacts with body adiposity and negatively affects glucose-stimulated GLP-1 (show GCG Proteins) levels, insulin (show INS Proteins) secretion, and glucose tolerance.
CUX-1 (show CUX1 Proteins) overexpression enhanced TNF (show TNF Proteins)- production on sCD26 (show CDC26 Proteins)/LPS (show IRF6 Proteins) stimulation, while CUX-1 (show CUX1 Proteins) depletion had no effect. Neither CUX-1 (show CUX1 Proteins) overexpression nor CUX-1 (show CUX1 Proteins) depletion had an effect on IL-6 (show IL6 Proteins) stimulation. These results are discussed in the context of a model that describes the mechanisms by which stimulation of monocytic cells by sCD26 (show CDC26 Proteins) and LPS (show IRF6 Proteins) leads to elevation of TNF (show TNF Proteins)- and IL-6 (show IL6 Proteins) expression.
Increased plasma DPP-4 activity may correlate with aneurysmal development. CD26 on monocytes plays a critical role in cell differentiation, possibly mediated by extracellular signal-regulated protein kinase (show CDK7 Proteins) 1/2-p21 (show CDKN1A Proteins) axis signaling pathways and cytoskeletal proteins reassembly.
Plasma DPP4 activity is significantly associated with NAFLD. The underlying mechanisms may be partly attributed to the interactions between insulin (show INS Proteins) resistance, oxidative stress, inflammation, and DPP4.
Results describe a proline-rich cytokine from neurosecretory granules that represents a new natural substrate for Dipeptidyl Peptidase IV (DPPIV).
Data demonstrate that dipeptidyl peptidase II (show DPP7 Proteins) can form a complex with adenosine deaminase (show ADA Proteins), but with one order of magnitude higher dissociation constant than that of DPPIV.
This study shows that porcine DPP-IV is generally inhibited with greater potency by protein-derived peptides than is the human enzyme
DPP-IV from porcine kidney cortex was characterized.
Neutral endopeptidase 24.11 (show MME Proteins) and DPP-IV is superior to DPP-IV inhibition alone in preserving intact GLP-1 (show GCG Proteins), which implies possibility that the combination has therapeutic potential.
Results describe the distribution of dipeptidyl peptidase IV-like activity enzymes in porcine tissue sections by RT-PCR.
systemic DPP4 inhibition restores the impaired mononuclear cell homing in Eng (show ENG Proteins)+/- animals post-myocardial infarction, and enhances cardiac repair, which might be explained by restoring the balance between the inflammatory and regenerative macrophages present in the heart
SGLT-2 (show SLC5A2 Proteins) inhibition with dapagliflozin reduces the activation of the Nlrp3 (show NLRP3 Proteins)/ASC (show STS Proteins) inflammasome and attenuates the development of diabetic cardiomyopathy in mice with type 2 diabetes. Effects are augmentated of the by DPP4 inhibitor Saxagliptin.
DPP-4 inhibitor teneligliptin inhibited atherogenesis in ApoE (show APOE Proteins) knockout mice, at least partially, through attenuation of the inflammatory phenotype of perivascular adipose tissue.
Increased plasma DPP-4 activity may correlate with aneurysmal development. CD26 on monocytes plays a critical role in cell differentiation, possibly mediated by extracellular signal-regulated protein kinase (show CDK7 Proteins) 1/2-p21 axis signaling pathways and cytoskeletal proteins reassembly.
High DPP4 expression is associated with cardiac ischemia and systolic dysfunction.
DPP4:CD9:TTSP (show TMPRSS11E Proteins) as the protein complexes are necessary for early efficient MERS-coronavirus entry.
these findings identify distinct roles for DPP4 in the endothelial cell versus the bone marrow compartment for selective incretin degradation and DPP4 inhibition-mediated glucoregulation.
The trimeric form receptor-binding domain of MERS-CoV spike protein bound strongly to the receptor of MERS-CoV, dipeptidyl peptidase 4 (DPP4), and elicited robust RBD (show CACNA1D Proteins)-specific neutralizing antibodies in mice.
the data show that glucose-induced expression of Dpp4 in the liver is facilitated by demethylation of the Dpp4 gene early in life. This might contribute to early deteriorations in hepatic function, which in turn result in metabolic disease such as hepatosteatosis later in life.
study reveals a cross talk between ATR signaling and DPP4 activation in the regulation of megalin (show LRP2 Proteins) and underscores the significance of targeting DPP4 in the prevention of obesity related kidney injury progression.
The protein encoded by this gene is identical to adenosine deaminase complexing protein-2, and to the T-cell activation antigen CD26. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides.
, DPP IV
, T-cell activation antigen CD26
, adenosine deaminase complexing protein 2
, dipeptidyl peptidase 4
, dipeptidyl peptidase IV
, dipeptidylpeptidase 4
, dipeptidylpeptidase IV (CD26, adenosine deaminase complexing protein 2)
, activation molecule 3
, adenosine deaminase complexing protein
, dipeptidyl-peptidase 4 (CD26, adenosine deaminase complexing protein 2)
, dipeptidyl-peptidase iv
, dipeptidyl-peptidase 4
, dipeptidyl-peptidase IV
, dipeptidylpeptidase IV
, thymocyte-activating molecule
, GP110 glycoprotein
, bile canaliculus domain-specific membrane glycoprotein