ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.

ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.

American journal of physiology. Cell physiology (2017-05-05)

Darrice S Montgomery, Ling Yu, Zinah M Ghazi, Tiffany L Thai, Otor Al-Khalili, He-Ping Ma, Douglas C Eaton, Abdel A Alli

PMID28468944

要旨

We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains are a family of ubiquitously expressed intracellular Ca

材料

製品番号

ブランド

製品内容

F1804

Sigma-Aldrich

モノクローナル抗FLAG^® M2抗体マウス宿主抗体, 1 mg/mL, clone M2, affinity isolated antibody, buffered aqueous solution (50% glycerol, 10 mM sodium phosphate, and 150 mM NaCl, pH 7.4)

A9477

Sigma-Aldrich

アルドステロン, ≥95% (HPLC)

A6060

Sigma-Aldrich

カルパインインヒビター II, powder