D3321
Dipeptidyl Peptidase VII human
recombinant, expressed in Sf9 cells
Synonym(s):
DPP7, Quiescent cell proline dipeptidase
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
3.4.14.-
Specific activity:
≥1,500 units/μg protein, ≥1500 units/μg protein
Recombinant:
expressed in Sf9 cells
shipped in
dry ice
recombinant
expressed in Sf9 cells
form
solution
specific activity
≥1,500 units/μg protein, ≥1500 units/μg protein
mol wt
89.1 kDa
relevant disease(s)
diabetes; cardiovascular diseases
storage temp.
−70°C
Quality Level
Related Categories
Application
Dipeptidyl Peptidase VII (DPP7), also known as DPP2 or quiescent cell proline dipeptidase, is a post-proline cleaving aminopeptidase that is expressed in quiescent lymphocytes . DPP7 is used to study the regulation of cell quiescence . Like DPP4, DPP7 may be useful in diabetes and vascular disease research .
Biochem/physiol Actions
DPP7 is essential for maintaining lymphocytes and fibroblasts in G(0). The inhibition of DPP7 results in apoptosis, which is mediated by the induction of c-Myc and p53 . DPP7 has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.
General description
Contains amino acids 29 to end with a C-terminal His tag, MW=89.1 kDa
Other Notes
One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.4 at 25 deg °C
Physical form
Supplied as a solution in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 220 mM imidazole, and 20% glycerol.
signalword
Danger
hcodes
Hazard Classifications
Eye Dam. 1 - Repr. 1B - Skin Corr. 1C
Storage Class
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
wgk
WGK 2
Regulatory Information
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Hennady P Shulha et al.
PLoS biology, 10(11), e1001427-e1001427 (2012-11-28)
Cognitive abilities and disorders unique to humans are thought to result from adaptively driven changes in brain transcriptomes, but little is known about the role of cis-regulatory changes affecting transcription start sites (TSS). Here, we mapped in human, chimpanzee, and
Lin Zhu et al.
The Journal of general and applied microbiology, 58(3), 199-209 (2012-08-11)
Proteolytic degradation is one of the serious bottlenecks limiting the yields of heterologous protein production by Aspergillus oryzae. In this study, we selected a tripeptidyl peptidase gene AosedD (AO090166000084) as a candidate potentially degrading the heterologous protein, and performed localization
Mahesh Kamate et al.
Neurology India, 60(3), 316-320 (2012-07-25)
Neuronal ceroid lipofuscinosis is a group of progressive neurodegenerative disorders characterized by accumulation of ceroid lipopigment in lysosomes in neurons and other cell types. This study is a retrospective review of charts of patients with a diagnosis of infantile and
Martin Kruse et al.
The Journal of general physiology, 140(2), 189-205 (2012-08-02)
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) regulates activities of numerous ion channels including inwardly rectifying potassium (K(ir)) channels, KCNQ, TRP, and voltage-gated calcium channels. Several studies suggest that voltage-gated potassium (K(V)) channels might be regulated by PI(4,5)P(2). Wide expression of K(V) channels in
Dipeptidyl peptidase 2 is an essential survival factor in the regulation of cell quiescence.
Mele DA, et al.
Cell Cycle, 15, 2425-2434 (2009)
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