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5.08409

Sigma-Aldrich

Bafilomycin A1

≥90% (HPLC), liquid,V-ATPase inhibitor, Calbiochem

Synonym(s):

InSolution Bafilomycin A1, Bafilomycin A1, ≥97% by HPLC InSolution, InSolution Bafilomycin A1, ≥97% by HPLC

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About This Item

Empirical Formula (Hill Notation):
C35H58O9
CAS Number:
88899-55-2
Molecular Weight:
622.83
MDL number:
MFCD06795130
UNSPSC Code:
12352200
NACRES:
NA.77

product name

Bafilomycin A1, InSolution, ≥90%, A macrolide antibiotic that acts as a specific inhibitor of vacuolar-type H+-ATPase

Quality Level

100

Assay

≥90% (HPLC)

form

liquid

shelf life

2 yr

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles
desiccated (hygroscopic)
protect from light

storage temp.

−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

InChI key

XDHNQDDQEHDUTM-JQWOJBOSSA-N

General description

A macrolide antibiotic that acts as a specific inhibitor of vacuolar-type H+-ATPase (V-type; Ki = 0.5 nM) and is a valuable tool for distinguishing among different types of ATPases. Reported to selectivity inhibit β-secretase, an enzyme involved in the processing of amyloid precursor protein (APP). Blocks lysosomal cholesterol trafficking in macrophages. Known to interfere with pH regulation in brain cells. Inhibits bone resorption both in vivo and in vitro. Has been shown to exhibit cytotoxic effects on a number of cell lines in a cell viability assay.

Biochem/physiol Actions

Cell permeable: yes
Primary Target
vacuolar-type H+-ATPase

Packaging

Packaged under inert gas

Warning

Toxicity: Standard Handling (A)

Reconstitution

Following initial thaw, aliquot and freeze (-20°C). Aliquots are stable for up to 1 year at -20°C. Use only fresh DMSO for further dilutions.

Other Notes

Sinha, S., and Lieberburg, I. 1999. Proc. Natl. Acad. Sci. USA96, 11049.
Calvert, C.M., and Sanders, D. 1995. J. Biol. Chem.270, 7272.
Nishihara, T., et al. 1995. Biochem. Biophys. Res. Commun.269, 255.
Crider, B.P., et al. 1994. J. Biol. Chem.269, 17379.
Palokangas, H., et al. 1994. J. Biol. Chem.269, 17577.
Sundquist, K.T., and Marks, S.C., Jr. 1994. J. Bone Miner. Res.9, 1575.
Drose, S., et al. 1993. Biochemistry32, 3902.
Furuchi, T., et al. 1993. J. Biol. Chem.268, 27345.
Bowman, E.J., et al. 1988. Proc. Natl. Acad. Sci. USA85, 7972.

Legal Information

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

188.6 °F - (refers to pure substance)

Flash Point(C)

87 °C - (refers to pure substance)

Certificates of Analysis (COA)

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K T Sundquist et al.
Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 9(10), 1575-1582 (1994-10-01)
It has been shown that a specific inhibitor of vacuolar H(+)-ATPases, bafilomycin A1, inhibits bone resorption by isolated chicken osteoclasts by blocking the proton pump in the ruffled border membrane. We report here the effects of bafilomycin A1 on bone
H Palokangas et al.
The Journal of biological chemistry, 269(26), 17577-17585 (1994-07-01)
Bafilomycin A1 (Baf), a specific inhibitor of the vacuolar-type proton pump, inhibited the entry of Semliki Forest virus and vesicular stomatitis virus into BHK-21 cells. The inhibition occurred at concentrations that dissipated intracellular acidic compartments. Viral infection was totally inhibited
B P Crider et al.
The Journal of biological chemistry, 269(26), 17379-17381 (1994-07-01)
Vacuolar-type proton-translocating ATPases are complex heterooligomers that are characterized by a specific inhibition by bafilomycin A1. These enzymes have a peripheral ATP hydrolytic domain as well as a transmembranous sector. The transmembranous sector has been isolated by glycerol gradient centrifugation
T Furuchi et al.
The Journal of biological chemistry, 268(36), 27345-27348 (1993-12-25)
Certain steroids having an oxo group at the C-17 or C-20 position such as pregnenolone and dehydroisoandrosterone inhibit the cholesterol transport from lysosomes to other cellular sites. Taking advantage of the fact that the inhibition is reversed upon removal of
C M Calvert et al.
The Journal of biological chemistry, 270(13), 7272-7280 (1995-03-31)
Vacuolar membrane vesicles were isolated from Candida albicans protoplasts, and marker enzyme assays were employed to identify the membranes as vacuolar in origin. The mechanisms of Ca2+ uptake and Ca2+ release at the vacuolar membrane were investigated. Ca2+ accumulation by
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