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EMU207441

Sigma-Aldrich

MISSION® esiRNA

targeting mouse Ifitm3

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About This Item

UNSPSC Code:
41105324
NACRES:
NA.51

description

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Quality Level

product line

MISSION®

form

lyophilized powder

esiRNA cDNA target sequence

CCAAACTACGAAAGAATCAAGGAAGAATATGAGGTGGCTGAGATGGGGGCACCGCACGGATCGGCTTCTGTCAGAACTACTGTGATCAACATGCCCAGAGAGGTGTCGGTGCCTGACCATGTGGTCTGGTCCCTGTTCAATACACTCTTCATGAACTTCTGCTGCCTGGGCTTCATAGCCTATGCCTACTCCGTGAAGTCTAGGGATCGGAAGATGGTGGGTGATGTGACTGGAGCCCAGGCCTACGCCTCCACTGCTAAGTGCCTGAACATCAGCACCTTGGTCCTCAGCATCCTGATGGTTGTTATCACCATTGTTAGTGTCATCATCATTGTTCTTAACGCTCAAAACCTTCACACTTAATAGAGGATTCCGACTTCCGGTCCTGAAGTGCTTCACCCTCCGCAGCTGCGTCCCTCCTTGCCCCTCCCTACACGCAGGTGTAACACTCATTTATCTATCCACAGTGGATTCAATAAAGTGCA

Ensembl | mouse accession no.

NCBI accession no.

shipped in

ambient

storage temp.

−20°C

Gene Information

General description

MISSION® esiRNA are endoribonuclease prepared siRNA. They are a heterogeneous mixture of siRNA that all target the same mRNA sequence. These multiple silencing triggers lead to highly-specific and effective gene silencing.

For additional details as well as to view all available esiRNA options, please visit SigmaAldrich.com/esiRNA.

Legal Information

MISSION is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Milene Mesquita et al.
PloS one, 9(6), e101056-e101056 (2014-07-01)
HIV-1-infected patients co-infected with A(H1N1)pdm09 surprisingly presented benign clinical outcome. The knowledge that HIV-1 changes the host homeostatic equilibrium, which may favor the patient resistance to some co-pathogens, prompted us to investigate whether HIV-1 infection could influence A(H1N1)pdm09 life cycle
Nicholas M Chesarino et al.
PLoS pathogens, 11(8), e1005095-e1005095 (2015-08-12)
Interferon (IFN)-induced transmembrane protein 3 (IFITM3) is a cell-intrinsic factor that limits influenza virus infections. We previously showed that IFITM3 degradation is increased by its ubiquitination, though the ubiquitin ligase responsible for this modification remained elusive. Here, we demonstrate that

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