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Merck
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SML1845

Sigma-Aldrich

Thapsigargin Ready Made Solution

≥98% (HPLC), 10 mM in DMSO

Szinonimák:

CHEBI:9516, CHEMBL96926, MFCD00083511, UNII-Z96BQ26RZD, Z96BQ26RZD, [(3S,3aR,4S,6S,6aR,7S,8S,9bS)-6-acetyloxy-4-butanoyloxy-3,3a-dihydroxy-3,6,9-trimethyl-8-[(Z)-2-methylbut-2-enoyl]oxy-2-oxo-4,5,6a,7,8,9b-hexahydroazuleno[4,5-b]furan-7-yl] octanoate

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Összes fotó(1)

About This Item

Tapasztalati képlet (Hill-képlet):
C34H50O12
CAS-szám:
67526-95-8
Molekulatömeg:
650.75
UNSPSC kód:
12352200
NACRES:
NA.77

biológiai forrás

(Thapsia garganica L seeds)

Minőségi szint

200

Teszt

≥98% (HPLC)

form

DMSO solution

koncentráció

10 mM in DMSO

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

InChI

1S/C34H50O12/c1-9-12-13-14-15-17-24(37)43-28-26-25(20(5)27(28)44-30(38)19(4)11-3)29-34(41,33(8,40)31(39)45-29)22(42-23(36)16-10-2)18-32(26,7)46-21(6)35/h11,22,26-29,40-41H,9-10,12-18H2,1-8H3/b19-11-/t22-,26+,27-,28-,29-,32-,33+,34+/m0/s1

Nemzetközi kémiai azonosító kulcs

IXFPJGBNCFXKPI-FSIHEZPISA-N

Alkalmazás

Thapsigargin Ready Made Solution has been used as a negative control in in vivo growth and in vitro translation measurements.

Biokémiai/fiziológiai hatások

Thapsigargin is an effective inhibitor of calcium ion pumps located on sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) microsomes of skeletal, cardiac, muscle and brain tissues. The inhibition of calcium ion pumps causes intracellular increase of calcium ion levels. It was found that thapsigargin at 100 nM concentration effectively inhibited the SR Ca2+- adenosine triphosphatase (ATPase) in cardiac and skeletal muscles. Thapsigargin was also reported to be effective in blocking autophagy by interfering with the autophagosome-lysosome fusion.
Thapsigargin is an effective inhibitor of calcium ion pumps located on sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) microsomes of skeletal, cardiac, muscle and brain tissues.

Egyéb megjegyzések

Thapsigargin Ready Made Solution is provided at 10 mM concentration in DMSO. The solution can be further diluted with DMSO to a concentration of 2 mM. It is recommended to store Thapsigargin Ready Made Solution in small aliquots at -20 °C.

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 2

Lobbanási pont (F)

188.6 °F - closed cup

Lobbanási pont (C)

87 °C - closed cup

Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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2-APB A cell-permeable modulator of Ins(1,4,5)P3-induced Ca2+ release.

Sigma-Aldrich

100065

2-APB

Brefeldin A from Penicillium brefeldianum, ≥99% (HPLC and TLC)

Sigma-Aldrich

B7651

Brefeldin A

Sodium tauroursodeoxycholate

Sigma-Aldrich

T0266

Sodium tauroursodeoxycholate

Thapsigargin blocks the induction of long-term potentiation in rat hippocampal slices
<BIG>Harvey J and Collingridge GL</BIG>
Neuroscience Letters, 197-200 (1992)
M Alsaqati et al.
British journal of pharmacology, 171(3), 701-713 (2013-10-22)
The P2Y₁₄ receptor is the newest member of the P2Y receptor family; it is G(i/o) protein-coupled and is activated by UDP and selectively by UDP-glucose and MRS2690 (2-thiouridine-5'-diphosphoglucose) (7-10-fold more potent than UDP-glucose). This study investigated whether P2Y₁₄ receptors were
J Lytton et al.
The Journal of biological chemistry, 266(26), 17067-17071 (1991-09-15)
The role of ATP-dependent calcium uptake into intracellular storage compartments is an essential feature of hormonally induced calcium signaling. Thapsigargin, a non-phorboid tumor promoter, increasingly is being used to manipulate calcium stores because it induces a hormone-like elevation of cytosolic
Partial inactivation of cardiac 14-3-3 protein in vivo elicits endoplasmic reticulum stress (ERS) and activates ERS-initiated apoptosis in ERS-induced mice
<BIG>Sari FR, et al.</BIG>
Cellular Physiology and Biochemistry, 167-178 (2010)
Kevin Shenderov et al.
Journal of immunology (Baltimore, Md. : 1950), 192(5), 2029-2033 (2014-02-04)
The accumulation of improperly folded proteins within the endoplasmic reticulum (ER) generates perturbations known as ER stress that engage the unfolded protein response. ER stress is involved in many inflammatory pathologies that are also associated with the production of the
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