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EHU081781

Sigma-Aldrich

MISSION® esiRNA

targeting human ST3GAL1

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About This Item

UNSPSC Code:
41105324
NACRES:
NA.51

description

Powered by Eupheria Biotech

product line

MISSION®

form

lyophilized powder

esiRNA cDNA target sequence

ATGTGGACCCTATGCTGGAGAAGAGGTCGGTGGGCTGCCGGCGCTGCGCCGTTGTGGGCAACTCGGGCAACCTGAGGGAGTCTTCTTATGGGCCTGAGATAGACAGTCACGACTTTGTCCTCAGGATGAACAAGGCGCCCACGGCAGGGTTTGAAGCTGATGTTGGGACCAAGACCACCCACCATCTGGTGTACCCTGAGAGCTTCCGGGAGCTGGGAGATAATGTCAGCATGATCCTGGTGCCCTTCAAGACCATCGACTTGGAGTGGGTGGTGAGCGCCATCACCACGGGCACCATTTCCCACACCTACATCCCGGTTCCTGCAAAGATCAGAGTGAAACAGGATAAGATCCTGATCTACCACCCAGCCTTCATCAAGTATGTCTTTGACAACTGGCTGCA

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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Tan-Chi Fan et al.
Cancer letters, 434, 184-195 (2018-07-25)
GFRA1 and RET are overexpressed in estrogen receptor (ER)-positive breast cancers. Binding of GDNF to GFRA1 triggers RET signaling leading to ER phosphorylation and estrogen-independent transcriptional activation of ER-dependent genes. Both GFRA1 and RET are membrane proteins which are N-glycosylated
Wen-Der Lin et al.
Cancer immunology research, 9(1), 113-122 (2020-11-13)
Altered glycosylations, which are associated with expression and activities of glycosyltransferases, can dramatically affect the function of glycoproteins and modify the behavior of tumor cells. ST3GAL1 is a sialyltransferase that adds sialic acid to core 1 glycans, thereby terminating glycan

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