Size : | Price | Quantity | |
---|---|---|---|
1 mg | $70.00 | ||
5 mg | $310.00 |
Historically isolated from Kitasatosporia kifunense.1 Kifunensine (CAS 109944-15-2) is an inhibitor of class I α-mannosidases which inhibit glycoprotein processing. Inhibits human endoplasmic reticulum α-1,2-mannosidase I and Golgi Class I mannosidases IA, IB and IC with Ki values of 130 and 23 nM respectively.2 Inhibition of endoplasmic reticulum a-mannosidase I activity rescues the human a-sarcoglycan R77C mutation suggesting a new pharmacological approach for limb girdle muscular dystrophy type 2D patients carrying mutations that impair a-sarcoglycan trafficking.3 Improves maturation of misfolded proteins.4
References/Citations:
1) Iwami et al. (1987), A new immunomodulator, FR-900494: taxonomy, fermentation, isolation, and physico-chemical and biological characteristics; J.Antibiot. (Tokyo) 40 612
2) Elbein et al. (1990), Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I; J.Biol.Chem. 265 15599
3) Bartoli et al. (2008), Mannosidase I inhibition rescues the human alpha-sarcoglycan R77C recurrent mutation; Hum.Mol.Genet. 17 1214
4) Wang et al. (2011), Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases; J.Biol.Chem. 286 43454
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Historically isolated from Kitasatosporia kifunense.1 Kifunensine (CAS 109944-15-2) is an inhibitor of class I α-mannosidases which inhibit glycoprotein processing. Inhibits human endoplasmic reticulum α-1,2-mannosidase I and Golgi Class I mannosidases IA, IB and IC with Ki values of 130 and 23 nM respectively.2 Inhibition of endoplasmic reticulum a-mannosidase I activity rescues the human a-sarcoglycan R77C mutation suggesting a new pharmacological approach for limb girdle muscular dystrophy type 2D patients carrying mutations that impair a-sarcoglycan trafficking.3 Improves maturation of misfolded proteins.4
References/Citations:
1) Iwami et al. (1987), A new immunomodulator, FR-900494: taxonomy, fermentation, isolation, and physico-chemical and biological characteristics; J.Antibiot. (Tokyo) 40 612
2) Elbein et al. (1990), Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I; J.Biol.Chem. 265 15599
3) Bartoli et al. (2008), Mannosidase I inhibition rescues the human alpha-sarcoglycan R77C recurrent mutation; Hum.Mol.Genet. 17 1214
4) Wang et al. (2011), Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases; J.Biol.Chem. 286 43454
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