Conserved Oligomeric Golgi complex 6 (COG6), also known as COD2, is a member of the conserved oligomeric Golgi (COG) complex. COG complex is composed of eight distinct subunits organized in two heterotrimeric groups, Cog2-Cog3- Cog4 and Cog5-Cog6-Cog7, which are linked by the dimeric group formed by Cog1 and Cog8.
Immunogen
a peptide corresponding to the C-terminal region of human COG6, conjugated to KLH. The corresponding sequence differs by three amino acids in mouse and rat COG6.
Application
Anti-COG6 (C-terminal) antibody produced in rabbit has been used in various immunochemical techniques including immunoblotting and immunoprecipitation.
Biochem/physiol Actions
COG complex is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking and maintenance of Golgi glycosylation machinery in eukaryotic cells. COG complex interacts directly with the target membrane (t-SNARE) Syntaxin 6 through COG6 subunit. COG6-depleted cells display reduced steady-state level of Syntaxin 6 and attenuated endosome-to- trans‐Golgi network (TGN) retrograde trafficking. Deficiency of COG6 causes a combined N- and Oglycosylation deficiency of the congenital disorders of glycosylation, designated as CDG-IIL (COG6- congenital disorders of glycosylation (CDG)).
Physical form
Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.
The Journal of cell biology, 194(3), 459-472 (2011-08-03)
The conserved oligomeric Golgi (COG) complex has been implicated in the regulation of endosome to trans-Golgi network (TGN) retrograde trafficking in both yeast and mammals. However, the exact mechanisms by which it regulates this transport route remain largely unknown. In
Human molecular genetics, 19(18), 3623-3633 (2010-07-08)
Deficiency of subunit 6 of the conserved oligomeric Golgi (COG6) complex causes a new combined N- and O-glycosylation deficiency of the congenital disorders of glycosylation, designated as CDG-IIL (COG6-CDG). The index patient presented with a severe neurologic disease characterized by
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