D3571
Dipeptidyl Peptidase III human
recombinant, expressed in Sf9 cells
Sinónimos:
DPP III
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About This Item
NACRES:
NA.54
UNSPSC Code:
12352204
Nombre del producto
Dipeptidyl Peptidase III human, recombinant, expressed in Sf9 cells
recombinant
expressed in Sf9 cells
form
solution
specific activity
≥400 units/μg protein
mol wt
82 kDa
concentration
≥0.1 mg/mL
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
human ... DPP3(10072)
Categorías relacionadas
Application
Human dipeptidyl peptidase III has been used in a study to assess the effect of entropy-driven binding of opioid peptides on large domain motion in human dipeptidyl peptidase III. Human dipeptidyl peptidase III has also been used in a study to investigate Ets-1/Elk-1 as a critical mediator of its transcription in human glioblastoma cells.
Biochem/physiol Actions
DPP III is a cytosolic zinc-exopeptidase that is involved in the intracellular protein catabolism of eukaryotes. The enzyme is a monomeric acidic protein with a molecular mass of approximately 82,000 Da and a pI of 4.5-4.6. It is sensitive to freezing and temperatures above 40 °C. It is found to be inhibited by metallo-chelators and sulfydryl reagents. The activity can be restored by divalent cations and thiol compounds. It has a particularly high affinity for angiotensin III. It acts as a post-proline-cleaving enzyme on endomorphins.
Other Notes
One unit will hydrolyze 1.0 picomole of Arg-Arg-AMC per minute at pH 7.5 at 25 deg °C
Physical form
Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 18 mM glutathione, 10% glycerol and 3 mM DTT.
Clase de almacenamiento
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Antonija Tomić et al.
Journal of molecular recognition : JMR, 24(5), 804-814 (2011-08-04)
Human dipeptidyl peptidase III (DPP III) is a zinc-exopeptidase with implied roles in protein catabolism, pain modulation, and defense against oxidative stress. To understand the mode of ligand binding into its active site, we performed molecular modeling, site-directed mutagenesis, and
Ashleigh M Philp et al.
International journal of molecular sciences, 22(13) (2021-07-03)
Obesity increases the risk of hip osteoarthritis (OA). Recent studies have shown that adipokine extracellular nicotinamide phosphoribosyltransferase (eNAMPT or visfatin) induces the production of IL-6 and matrix metalloproteases (MMPs) in chondrocytes, suggesting it may promote articular cartilage degradation. However, neither
Abhay A Shukla et al.
The FEBS journal, 277(8), 1861-1875 (2010-03-20)
Dipetidyl-peptidase III is a metallopeptidase involved in a number of physiological processes and its expression has been reported to increase with the histological aggressiveness of human ovarian primary carcinomas. Because no information regarding the regulation of its expression was available
Simon Stenberg et al.
eLife, 11 (2022-07-09)
Deletion of mitochondrial DNA in eukaryotes is currently attributed to rare accidental events associated with mitochondrial replication or repair of double-strand breaks. We report the discovery that yeast cells arrest harmful intramitochondrial superoxide production by shutting down respiration through genetically
M Abramić et al.
Biological chemistry Hoppe-Seyler, 369(1), 29-38 (1988-01-01)
Purification procedure for dipeptidyl peptidase III (DPP III) from human erythrocytes cytosol, entailing separations on DEAE-cellulose, hydroxylapatite and Sephacryl S-200 column, which gave homogeneous preparation in 35% yield, is described. The enzyme was shown to be a monomeric acidic protein
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