製品名
ジペプチジルペプチダーゼIII ヒト, 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)
関連するカテゴリー
Other Notes
1 unitは、pH 7.5、25°C、1分間に、1.0 pmolのArg-Arg-AMCを加水分解する酵素量です。
Physical form
25 mM Tris-HCl(pH 8.0)、100 mM NaCl、0.05% Tween-20、50% グリセロール、3 mM DTTで調製した溶液。
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.
保管分類
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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
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
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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