D3571
Dipeptidyl Peptidase III human
recombinant, expressed in Sf9 cells
别名:
DPP III
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关于此项目
NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥400 units/μg protein
Recombinant:
expressed in Sf9 cells
Concentration:
≥0.1 mg/mL
产品名称
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)
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.
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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
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
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
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
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
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