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581004

Sigma-Aldrich

Telomerase Inhibitor III, Sodium Salt

The Telomerase Inhibitor III, Sodium Salt controls the biological activity of Telomerase. This small molecule/inhibitor is primarily used for Cell Structure applications.

Synonym(s):

TAG-6, 5ʹ-d(TTAGGG)-3ʹ

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About This Item

UNSPSC Code:
12352200

Quality Level

form

lyophilized

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)
protect from light

solubility

water: soluble

shipped in

wet ice

storage temp.

−70°C

General description

A short, cell-permeable hexameric phosphorothioate oligonucleotide (PS-ODN) telomer mimic that inhibits telomerase activity in cell lysates and lengthens cell doubling time in vitro and in vivo at concentrations of less than 2.5 µM.
A short, cell-permeable hexameric phosphorothioate oligonucleotide (PS-ODN) telomere mimic that inhibits telomerase activity in cell lysates and lengthens cell doubling time in vitro and in vivo at concentrations of less than 2.5 µM. Note: 150 nmol = 285 µg.
M.W. ~1900.

Biochem/physiol Actions

Cell permeable: yes
Primary Target
Telomerase activity in cell lysates
Product competes with ATP.
Reversible: no

Packaging

Packaged under inert gas

Warning

Toxicity: Harmful & Carcinogenic / Teratogenic (E)

Sequence

5′-d(TTAGGG)-3′

Other Notes

Mata, J.E., et al. 1997. Toxicol. Appl. Pharmacol. 144, 189.

Legal Information

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Manuel Bernabé-García et al.
Molecular oncology, 15(7), 1818-1834 (2021-03-14)
Telomerase reverse transcriptase (TERT) maintains telomere homeostasis, thus ensuring chromosome stability and cell proliferation. In addition, several telomere-independent functions of human TERT have been described. In this study, we report that TERT binds directly to the TCF binding elements located

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