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Key Documents

D3571

Sigma-Aldrich

Dipeptidyl Peptidase III human

recombinant, expressed in Sf9 cells

Sinónimos:

DPP III

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Sf9 cells

Quality Level

form

solution

specific activity

≥400 units/μg protein

mol wt

82 kDa

concentration

≥0.1 mg/mL

NCBI accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... DPP3(10072)

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.

Unit Definition

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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

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
Marina Barsun et al.
Biological chemistry, 388(3), 343-348 (2007-03-07)
Dipeptidyl peptidase III (DPP III) is a zinc exopeptidase with an implied role in the mammalian pain-modulatory system owing to its high affinity for enkephalins and localisation in the superficial laminae of the spinal cord dorsal horn. Our study revealed
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

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