Lec1 Hamster Ovary Cells

Lec1 (formerly known as Pro-5wgaR1 3C) is a malt agglutinin resistant mutant selected from the proline-deficient CHO clone Pro-5. Lec1 lacks a glycosyltransferase called GlcNAc-T1, so N-linked carbohydrates are blocked at the intermediate of Man5GlcNAc2Asn. These cells are very useful for studying the effects of N-linked glycosylation changes on the function and compartmentalization of endogenous glycoprotein or virus infection and glycoprotein produced by cloning DNA transfection. It was put into storage after identification without mycoplasma.

Animal species/Organism Chinese hamster

Tissue and Cell Type Ovary

Morphology epithelial cell-like, adherent growth

Culture media and additives/Complete Growth Medium and Culture Conditions:

90% α MEM (MD0800)+10% fetal bovine serum (SD0200)+inositol 43.2mg/L (SD0014)+folic acid 8.82mg/L (SD0016)+ β- Mercaptoethanol 7.8mg/L (SD0031)+G/A (SD0038)

Complete medium: α MEM complete medium (article number: MD0807)

Gas phase: air, 95%; Carbon dioxide, 5%. Temperature: 37 ℃.

Freezing conditions: basic medium+5% DMSO+20% FBS (SD0200)

Complete cryopreservation solution: non-programmed cooling cell cryopreservation solution (low serum) (SD0001)

Note: This product is for scientific research only

PubMed=1182798; DOI=10.1016/0092-8674(75)90002-1

Stanley P., Caillibot V., Siminovitch L.

Selection and characterization of eight phenotypically distinct lines of lectin-resistant Chinese hamster ovary cell.

Cell 6:121-128(1975)

PubMed=3785164; DOI=10.1128/MCB.6.4.1268

Ripka J., Shin S.-I., Stanley P.

Decreased tumorigenicity correlates with expression of altered cell surface carbohydrates in Lec9 CHO cells.

Mol. Cell. Biol. 6:1268-1275(1986)

PubMed=8910379; DOI=10.1074/jbc.271.44.27818

Puthalakath H., Burke J., Gleeson P.A.

Glycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene.

J. Biol. Chem. 271:27818-27822(1996)

PubMed=24078077; DOI=10.1007/s00418-013-1146-1

Dong Z., Zuber C., Pierce M., Stanley P., Roth J.

Reduction in Golgi apparatus dimension in the absence of a residential protein, N-acetylglucosaminyltransferase V.

Histochem. Cell Biol. 141:153-164(2014)