DPP8 peptide

Name: DPP8 peptide
SKU: DAG-P1535
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Nature

Synthetic

Tag/Conjugate

Unconjugated

Purity

> 95 % by SDS-PAGE.

Format

Lyophilized

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles. Preservative: None Constituents: 0.001% Tween 20, 30mM HEPES, 2mM EDTA, 150mM Sodium chloride, pH 6.75

Reconstitution

DPP8 peptide is supplied as 1mg of dried peptide. When the peptide is reconstituted in 1 mL strile water, the concentration will be 1 mg/mL.

Introduction

This gene encodes a member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond. The encoded protein shares similarity with dipeptidyl peptidase IV in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]

Entrez Gene ID

54878

Synonyms

DPP8; dipeptidyl-peptidase 8; DP8; DPRP1; MSTP141; dipeptidyl peptidase 8; DPRP-1; DPP VIII; dipeptidylpeptidase 8; prolyl dipeptidase DPP8; dipeptidyl peptidase VIII; dipeptidyl peptidase IV-related protein 1; dipeptidyl peptidase IV-related protein-1;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Small molecule carbazole-based diketopyrrolopyrroles with tetracyanobutadiene acceptor unit as a non-fullerene acceptor for bulk heterojunction organic solar cells

JOURNAL OF MATERIALS CHEMISTRY A

Authors: Patil, Yuvraj; Misra, Rajneesh; Keshtov, M. L.; Sharma, Ganesh D.

Abstract

Herein, we investigated the photovoltaic properties of carbazole-based diketopyrrolopyrroles with tetracyanobutadiene acceptor units as highly efficient non-fullerene acceptors together with a D-A conjugated polymer, P, as a donor for polymer solar cells. After optimization, i.e. donor to acceptor weight ratio and solvent vapour annealing, the polymer solar cells exhibited power conversion efficiencies of up to 4.86% and 7.19% for DPP7 and DPP8 as acceptors, respectively. These results indicate that slight changes in the chemical structure of the small acceptor molecule significantly increase the efficiency of the device. The design and synthesis of these non-fullerene acceptors with broader absorption spectra extended towards the near infrared region may be key for the further development of high-performance and cost-effective solution-processed organic solar cells.

Decrease of the pro-inflammatory M1-like response by inhibition of dipeptidyl peptidases 8/9 in THP-1 macrophages - quantitative proteomics of the proteome and secretome

MOLECULAR IMMUNOLOGY

Authors: Suski, Maciej; Wisniewska, Anna; Kus, Katarzyna; Kiepura, Anna; Stachowicz, Aneta; Stachyra, Kamila; Czepiel, Klaudia; Madej, Jozef; Olszanecki, Rafal

Abstract

Background: Cellular peptidases are an emerging target of novel pharmacological strategies in inflammatory diseases and cancer. In this context, the dipeptidyl peptidases 8 and 9 (DPP8/9) have gained special attention due to their activities in the immune cells. However, in spite of more than hundred protein substrates identified to date by mass spectrometry-based analysis, the cellular DPP8/9 functions are still elusive. Methods: We applied the proteomic approach (iTRAQ-2DLC-MS/MS) to comprehensively analyze the role of DPP8/9 in the regulation of macrophage activation by in-depth protein quantitation of THP-1 proteome and secretome. Results: Cells pre-incubated with DPP8/9 inhibitor (1G244) prior activation (LPS or IL-4/IL-13) diminished the expression levels of M1-like response markers, but not M2-like phenotype features. This was accompanied by multiple intra- and extra-cellular protein abundance changes in THP-1 cells, related to cellular metabolism, mitochondria and endoplasmic reticulum function, as well as those engaged with inflammatory and apoptotic processes, including previously reported and novel DPP8/9 targets. Conclusions: Inhibition of DPP 8/9 had a profound effect on the THP-1 macrophage proteome and secretome, evidencing the decrease of the pro-inflammatory M1-like response. Presented results are to our best knowledge the first which, among others, highlight the metabolic effects of DPP8/9 inhibition in macrophages.