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Merck
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Fontos dokumentumok

5.08409

Sigma-Aldrich

Bafilomycin A1

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

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Tapasztalati képlet (Hill-képlet):
C35H58O9
CAS-szám:
Molekulatömeg:
622.83
MDL-szám:
UNSPSC kód:
12352200
NACRES:
NA.77

product name

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

Minőségi szint

Teszt

≥90% (HPLC)

form

liquid

eltarthatósági idő

2 yr

gyártó/kereskedő neve

Calbiochem®

tárolási körülmény

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

tárolási hőmérséklet

−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

Nemzetközi kémiai azonosító kulcs

XDHNQDDQEHDUTM-JQWOJBOSSA-N

Általános leírás

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.

Biokémiai/fiziológiai hatások

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

Kiszerelés

Packaged under inert gas

Figyelmeztetés

Toxicity: Standard Handling (A)

Feloldás

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.

Egyéb megjegyzések

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.

Jogi információk

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

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1

Lobbanási pont (F)

188.6 °F - (refers to pure substance)

Lobbanási pont (C)

87 °C - (refers to pure substance)


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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Dokumentumtár megtekintése

Az ügyfelek ezeket is megtekintették

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
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
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
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
S Sinha et al.
Proceedings of the National Academy of Sciences of the United States of America, 96(20), 11049-11053 (1999-09-29)
The major constituent of senile plaques in Alzheimer's disease is a 42-aa peptide, referred to as beta-amyloid (Abeta). Abeta is generated from a family of differentially spliced, type-1 transmembrane domain (TM)-containing proteins, called APP, by endoproteolytic processing. The major, relatively

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