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Data on the inhibition of RNase inhibitor activity by a monoclonal antibody as assessed by microfluidics-based RNA electrophoresis.
Wang, Xiao; Teferedegne, Belete; Shatzkes, Kenneth; Tu, Wei; Murata, Haruhiko.
Afiliação
  • Wang X; Laboratory of DNA Viruses, Division of Viral Products, OVRR, CBER, FDA, Silver Spring, MD 20993, USA.
  • Teferedegne B; Laboratory of DNA Viruses, Division of Viral Products, OVRR, CBER, FDA, Silver Spring, MD 20993, USA.
  • Shatzkes K; Laboratory of DNA Viruses, Division of Viral Products, OVRR, CBER, FDA, Silver Spring, MD 20993, USA.
  • Tu W; Laboratory of DNA Viruses, Division of Viral Products, OVRR, CBER, FDA, Silver Spring, MD 20993, USA.
  • Murata H; Laboratory of DNA Viruses, Division of Viral Products, OVRR, CBER, FDA, Silver Spring, MD 20993, USA.
Data Brief ; 9: 417-421, 2016 Dec.
Article em En | MEDLINE | ID: mdl-27699193
ABSTRACT
Using purified reaction components, a commercial monoclonal antibody (Ab) specific to RNase inhibitor (RI) was found to interfere with the activity of RI. Total RNA was mixed with a monoclonal Ab specific to either RI (clone 3F11) or glyceraldehyde-3-phosphate dehydrogenase (GAPDH), RNase A, RI, or a combination of the above. Following incubation for 1 h at 22 °C or 37 °C, RNA integrity of the mixtures was assessed using microfluidics-based Bio-Rad Experion RNA electrophoresis. The addition of Ab 3F11 prevented RI from effectively inhibiting RNase A and therefore resulted in extensive RNA degradation. The data presented are associated with the research article entitled "Endogenous RNase Inhibitor Contributes to Stability of RNA in Crude Cell Lysates Applicability to Reverse Transcription Quantitative PCR (RT-qPCR)" (Wang et al., 2016) [1].
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Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Data Brief Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Data Brief Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Estados Unidos