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EHU032411

Sigma-Aldrich

MISSION® esiRNA

targeting human STAM

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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

CAACATGAAGGCCGAAAAGTTCGTGCTATATATGACTTTGAAGCTGCTGAAGACAATGAACTTACTTTTAAAGCTGGAGAAATTATTACAGTTCTTGATGACAGTGATCCTAACTGGTGGAAAGGTGAAACCCATCAAGGCATAGGGTTATTTCCTTCTAATTTTGTGACTGCAGATCTCACTGCTGAACCAGAAATGATTAAAACAGAGAAGAAGACGGTACAATTTAGTGATGATGTTCAGGTAGAGACAATAGAACCAGAGCCGGAACCAGCCTTTATTGATGAAGATAAAATGGACCAGTTGCTACAGATGCTGCAAAGTACAGACCCCAGTGATGATCAGCCAGACCTACCAGAGCTGCTTCATCTTGAAGCAATGTGTCACCAGATGGGACCTCTCATTGATGAAAAGCTGGAAGATATTGATAGAAAACATTCAGAACTCTCAGAACTTAATGTGAAAGTGATGGAGGCC

Ensembl | human 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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Rutuja Kulkarni et al.
Scientific reports, 7(1), 14787-14787 (2017-11-03)
Exosomes are membrane enclosed nano-sized vesicles actively released into the extracellular milieu that can harbor genomic, proteomic and lipid cargos. Functionally, they are shown to regulate cell-cell communication and transmission of pathogens. Though studies have implicated a role for exosomes
Olga Alekhina et al.
The Journal of biological chemistry, 291(50), 26083-26097 (2016-10-30)
The chemokine receptor CXCR4 and its chemokine ligand CXCL12 mediate directed cell migration during organogenesis, immune responses, and metastatic disease. However, the mechanisms governing CXCL12/CXCR4-dependent chemotaxis remain poorly understood. Here, we show that the β-arrestin1·signal-transducing adaptor molecule 1 (STAM1) complex

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