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Description:
Slc9a9 (Sodium/hydrogen exchanger 9) or NHE9 may act in electroneutral exchange of protons for Na(+) across membranes. Four isoforms of the Na+/H+ exchanger (NHE6-NHE9) are distributed to intracellular compartments in human cells. They are localized to Golgi and post-Golgi endocytic compartments as follows: mid- to trans-Golgi, NHE8; trans-Golgi network, NHE7; early recycling endosomes, NHE6; and late recycling endosomes, NHE9. The intracellular localization of the NHEs is established by the balance of transport in and out of the post-Golgi compartments as the dynamic membrane trafficking. Their in vivo function is to regulate the pH and monovalent cation concentration in these organelles.
Description:
A readily soluble, specific and sensitive substrate for chymotrypsin and human pancreatic elastase. It is also hydrolyzed by cathepsin G and chymase. Furthermore it is the standard substrate for FK-506 binding proteins (FKBPs, also called macrophilins) and cyclophilins, which belong to the group of peptidyl prolyl cis-trans isomerases (PPIases). Thus, Suc-AAPF-pNA has been used for an uncoupled protease-free assay of PPIase activity.
Description:
PACS proteins are involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. PACS-1, or Phosphofurin acidic cluster sorting protein 1, is involved in protein sorting and ion channel trafficking. It directs the trans-Golgi network (TGN) localization of furin and M6PR (Mannose 6-phosphate receptor). PACS-1 also mediates the binding of VAMP4, a TGN-to-endosome transport protein, to AP-1.
Description:
Cyclophilins facilitate the process of protein folding. They catalyzes the cis-trans isomerization of proline imidic peptide bonds. Cyclophilin F is located in mitochondrion matrix. Cyclophilin F is involved in regulation of the mitochondrial permeability transition pore. It may activate or inhibit apoptosis or necrosis. It binds to an immunosuppressant cyclosporin.
Description:
Suc-ALPF-pNA, substrate for FK-506 binding proteins (FKBPs, also called macrophilins) and cyclophilins, which belong to the group of peptidyl prolyl cis-trans isomerases (PPIases). This tetrapeptide has been used for an uncoupled protease-free assay of PPIase activity.