422500
Kifunensine, Kitasatosporia kifunense
A potent alkaloid inhibitor of mannosidase I.
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Synonym(s):
Kifunensine, Kitasatosporia kifunense
Empirical Formula (Hill Notation):
C8H12N2O6
Recommended Products
Quality Level
Assay
≥98% (TLC)
form
solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
desiccated (hygroscopic)
color
white
solubility
hot water: 25 mg/mL
shipped in
ambient
storage temp.
−20°C
InChI
1S/C8H12N2O6/c11-1-2-3(12)4(13)5(14)6-9-7(15)8(16)10(2)6/h2-6,11-14H,1H2,(H,9,15)/t2-,3-,4+,5+,6+/m1/s1
InChI key
OIURYJWYVIAOCW-PQMKYFCFSA-N
General description
A potent alkaloid inhibitor of mannosidase I. An ineffective inhibitor of mannosidase II and the endoplasmic reticulum α-mannosidase.
A potent alkaloid inhibitor of mannosidase I. Does not affect mannosidase II and the endoplasmic reticulum α-mannosidase.
Biochem/physiol Actions
Cell permeable: no
Primary Target
mannosidase-1
mannosidase-1
Product does not compete with ATP.
Reversible: no
Warning
Toxicity: Standard Handling (A)
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Other Notes
Weng, S., and Spiro, R.G. 1996. Arch. Biochem. Biophys.325, 113.
Kayakiri, H., et al. 1991. Chem. Pharm. Bull. 39, 1378.
Elbein, A.D., et al. 1990. J. Biol. Chem. 265, 15599.
Iwami, M., et al. 1987. J. Antibiotic. 40, 612.
Kayakiri, H., et al. 1991. Chem. Pharm. Bull. 39, 1378.
Elbein, A.D., et al. 1990. J. Biol. Chem. 265, 15599.
Iwami, M., et al. 1987. J. Antibiotic. 40, 612.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Merve Sen et al.
Biomolecules, 11(10) (2021-10-24)
Rhodopsin (RHO) misfolding mutations are a common cause of the blinding disease autosomal dominant retinitis pigmentosa (adRP). The most prevalent mutation, RHOP23H, results in its misfolding and retention in the endoplasmic reticulum (ER). Under homeostatic conditions, misfolded proteins are selectively
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