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SML1661

Sigma-Aldrich

Bafilomycin A1

from Streptomyces griseus, ≥90% (HPLC), DMSO solution, V-ATPase inhibitor

Synonyme(s) :

BafA1

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About This Item

Formule empirique (notation de Hill):
C35H58O9
Numéro CAS:
88899-55-2
Poids moléculaire :
622.83
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77

product name

Bafilomycin A1 Ready Made Solution, 0.16 mM in DMSO, from Streptomyces griseus

Source biologique

Streptomyces griseus

Niveau de qualité

200

Forme

DMSO solution

Concentration

0.16 mM in DMSO

Conditions d'expédition

dry ice

Température de stockage

−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

Clé InChI

XDHNQDDQEHDUTM-JQWOJBOSSA-N

Description générale

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.

Application

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

Actions biochimiques/physiologiques

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.

Autres remarques

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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

188.6 °F - closed cup

Point d'éclair (°C)

87 °C - closed cup

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Consulter la Bibliothèque de documents

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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