Human DGKA ELISA Matched Antibody Pair

Name: Human DGKA ELISA Matched Antibody Pair
SKU: ABPR-0262
Rating: 5 (1 reviews)

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

COA

SDS

Datasheet

Summary

Species Reactivity

Human

Intended Use

This antibody pair set comes with matched antibody pair to detect and quantify protein level of human DGKA.

General Description

The protein encoded by this gene belongs to the eukaryotic diacylglycerol kinase family. It acts as a modulator that competes with protein kinase C for the second messenger diacylglycerol in intracellular signaling pathways. It also plays an important role in the resynthesis of phosphatidylinositols and phosphorylating diacylglycerol to phosphatidic acid. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.

Reconstitution And Storage

Store reagents of the antibody pair set at -20°C or lower. Please aliquot to avoid repeated freeze thaw cycle. Reagents should be returned to -20°C storage immediately after use.

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

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Customer Reviews

References

The Diacylglycerol Kinase alpha/Atypical PKC/beta 1 Integrin Pathway in SDF-1 alpha Mammary Carcinoma Invasiveness

PLOS ONE

Authors: Rainero, Elena; Cianflone, Cristina; Porporato, Paolo Ettore; Chianale, Federica; Malacarne, Valeria; Bettio, Valentina; Ruffo, Elisa; Ferrara, Michele; Benecchia, Fabio; Capello, Daniela; Paster, Wolfgang; Locatelli, Irene; Bertoni, Alessandra; Filigheddu, Nicoletta; Sinigaglia, Fabiola; Norman, Jim C.; Baldanzi, Gianluca; Graziani, Andrea

Abstract

Diacylglycerol kinase a (DGK alpha), by phosphorylating diacylglycerol into phosphatidic acid, provides a key signal driving cell migration and matrix invasion. We previously demonstrated that in epithelial cells activation of DGK alpha activity promotes cytoskeletal remodeling and matrix invasion by recruiting atypical PKC at ruffling sites and by promoting RCP-mediated recycling of alpha 5 beta 1 integrin to the tip of pseudopods. In here we investigate the signaling pathway by which DGK alpha mediates SDF-1 alpha-induced matrix invasion of MDA-MB-231 invasive breast carcinoma cells. Indeed we showed that, following SDF-1 alpha stimulation, DGKa is activated and localized at cell protrusion, thus promoting their elongation and mediating SDF-1 alpha induced MMP-9 metalloproteinase secretion and matrix invasion. Phosphatidic acid generated by DGK alpha promotes localization at cell protrusions of atypical PKCs which play an essential role downstream of DGK alpha by promoting Rac-mediated protrusion elongation and localized recruitment of beta 1 integrin and MMP-9. We finally demonstrate that activation of DGK alpha, atypical PKCs signaling and beta 1 integrin are all essential for MDA-MB-231 invasiveness. These data indicates the existence of a SDF-1 alpha induced DGK alpha - atypical PKC - beta 1 integrin signaling pathway, which is essential for matrix invasion of carcinoma cells.

ISKpn40-Mediated Mobilization of the Colistin Resistance Gene mcr-3.11 in Escherichia coli

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY

Authors: He, Yu-Zhang; Long, Teng-Fei; Chen, Cai-Ping; He, Bing; Li, Xing-Ping; Schuyler, Jessica; Chen, Liang; Liao, Xiao-Ping; Liu, Ya-Hong; Sun, Jian

Abstract

The mobile colistin resistance gene mcr-3 has globally disseminated since it was first reported in 2017 in Escherichia coll. In vitro mobilization assays in this study demonstrate the functionality of the composite transposon structure ISKpri40-mcr-3.11-dgkA-ISKpn40 in wild-type and recA - E. coli strains. These transpositions generated 4-bp duplications at the target sites. This is the first report demonstrating the mobility of the mcr-3.11 gene by transposition.