D3571

Sigma-Aldrich

Dipeptidyl Peptidase III human

recombinant, expressed in Sf9 cells

Synonym(s):
DPP III
NACRES:
NA.54

Quality Level

recombinant

expressed in Sf9 cells

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)

Related Categories

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_code

12 - Non Combustible Liquids

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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...
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...
Eve Lauren Grumish et al.
Visceral medicine, 36(3), 212-219 (2020-08-11)
Alcohol increases the risk of colon cancer. Colonic inflammation mediates the effects of alcohol on colon carcinogenesis. Circadian rhythm disruption enhances the alcohol's effect on colonic inflammation and cancer. Here, we investigate the diurnal variation of lymphocyte infiltration in the...
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...
Gustavo A Bezerra et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(17), 6525-6530 (2012-04-12)
Opioid peptides are involved in various essential physiological processes, most notably nociception. Dipeptidyl peptidase III (DPP III) is one of the most important enkephalin-degrading enzymes associated with the mammalian pain modulatory system. Here we describe the X-ray structures of human...

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