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Merck

SML1661

Sigma-Aldrich

Bafilomycin A1 Ready Made Solution

0.16 mM in DMSO, from Streptomyces griseus

Synonim(y):

BafA1

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About This Item

Wzór empiryczny (zapis Hilla):
C35H58O9
Numer CAS:
Masa cząsteczkowa:
622.83
Kod UNSPSC:
12352200
NACRES:
NA.77

pochodzenie biologiczne

Streptomyces griseus

Poziom jakości

Postać

DMSO solution

stężenie

0.16 mM in DMSO

Warunki transportu

dry ice

temp. przechowywania

−20°C

InChI

1S/C35H58O9/c1-19(2)32-24(7)27(36)18-35(40,44-32)26(9)31(38)25(8)33-28(41-10)14-12-13-20(3)15-22(5)30(37)23(6)16-21(4)17-29(42-11)34(39)43-33/h12-14,16-17,19,22-28,30-33,36-38,40H,15,18H2,1-11H3/b14-12+,20-13+,21-16+,29-17-/t22-,23+,24-,25-,26-,27+,28-,30-,31+,32+,33+,35+/m0/s1

Klucz InChI

XDHNQDDQEHDUTM-JQWOJBOSSA-N

Opis ogólny

Bafilomycin A1, a macrolide antibiotic, belongs to the pleomacrolides family. It acts as a potent and selective inhibitor of vacuolar-type H+-ATPase. BafA1 can inhibit the viability of MG63 osteosarcoma cells. It can also stimulate mitochondrial dysfunction. BafA1 inhibits the proliferation of different types of cancer cells.

Zastosowanie

Bafilomycin A1 has been used:
  • as an endosome acidification inhibitor to study the importance of endosome acidification in the extracellular vesicle uptake and cytosolic release of stably expressing NanoLuc luciferase-tagged Hsp70 (NLuc-Hsp70) in HeLa cells
  • as a vacuolar-type H+-ATPase (V-ATPase) inhibitor to study its effects on autophagic turnover of light chain 3 β (LC3-II) in mice
  • as an autophagy inhibitor to study its effects on primary rat liver sinusoidal endothelial cells (LSECs) defenestration

Działania biochem./fizjol.

Bafilomycin A1 inhibits autophagy. It may exhibit anti-tumorigenic, anti-parasitic, and anti-neurodegenerative effects. Bafilomycin A1, found in lysosomes and endosomes prevents the acidification of these cell organelles. It also participates in blocking autophagosome-lysosome fusion and autolysosome acidification, steps necessary for maintaining the autophagic flux and cellular homeostasis.
Bafilomycin A1 is a macrolide antibiotic. Bafilomycin A1 acts as a potent and selective inhibitor of vacuolar-type H+-ATPase.

Inne uwagi

Bafilomycin A1 solution is provided in concentration of 0.16 mM. Typical concentrations for use in cell culture are 50-100 nM.
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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

188.6 °F - closed cup

Temperatura zapłonu (°C)

87 °C - closed cup


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Daniel J Klionsky et al.
Autophagy, 4(7), 849-850 (2008-09-02)
Bafilomycin A(1) is a specific inhibitor of the vacuolar type H(+)-ATPase (V-ATPase) in cells, and inhibits the acidification of organelles containing this enzyme, such as lysosomes and endosomes. Recently, while editing and reviewing chapters on autophagy for Methods in Enzymology
Kaitlin Katsura et al.
Scientific reports, 12(1), 2820-2820 (2022-02-20)
As the hardest tissue in the human body, tooth enamel formation is a highly regulated process involving several stages of differentiation and key regulatory genes. One such gene, tryptophan-aspartate repeat domain 72 (WDR72), has been found to cause a tooth enamel defect
Célia Fourrier et al.
Biochemical and biophysical research communications, 534, 107-113 (2020-12-15)
Measurement of autophagic flux in vivo is critical to understand how autophagy can be used to combat disease. Neurodegenerative diseases have a special relationship with autophagy, which makes measurement of autophagy in the brain a significant research priority. Currently, measurement of
Xiaoying Luo et al.
Cell death & disease, 9(5), 576-576 (2018-05-16)
Autophagy, interacting with actin cytoskeleton and the NO-dependent pathway, may affect the phenotype and function of endothelial cells. Moreover, caveolin-1 (Cav-1), as a structure protein in liver sinusoidal endothelial cells (LSECs), is closely related to autophagy. Hence, we aim to
M Angeles Juanes et al.
The Journal of cell biology, 218(10), 3415-3435 (2019-09-01)
Focal adhesion (FA) turnover depends on microtubules and actin. Microtubule ends are captured at FAs, where they induce rapid FA disassembly. However, actin's roles are less clear. Here, we use polarization-resolved microscopy, FRAP, live cell imaging, and a mutant of

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