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Merck

SAB4200427

Sigma-Aldrich

Anti-COG8 (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Sinónimos:

Anti-CDG2H, Anti-COG complex subunit 8, Anti-Component of oligomeric golgi complex 8, Anti-conserved oligomeric Golgi complex subunit 8, Anti-conserved oligomeric golgi complex component 8, Anti-dependent on RIC1, AntiDOR1

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

antigen ~70 kDa

reactividad de especies

human

concentración

~1.0 mg/mL

técnicas

immunoprecipitation (IP): 5-10 μg using lysates of human HEK-293T cells
indirect immunofluorescence: 0.5-1.0 μg/mL using using human HeLa cells
western blot: 1-2 μg/mL using whole extracts of human HEK-293 cells

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... COG8(84342)

Descripción general

Conserved oligomeric Golgi complex 8 (COG8), also known as DOR1 or CDG2H, is a member of the conserved oligomeric Golgi (COG) complex. COG complex is composed of eight distinct subunits organized as heterotrimeric groups namely Cog2-Cog3-Cog4 and Cog5-Cog6-Cog7. They are interlinked by the dimeric group comprising Cog1 and Cog8.

Especificidad

Anti-COG8 (C-terminal) recognizes human COG8.

Inmunógeno

synthetic peptide corresponding to the C-terminal region of human COG8, conjugated to KLH

Aplicación

Anti-COG8 (C-terminal) antibody produced in rabbit may be used in:
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence

Acciones bioquímicas o fisiológicas

COG complex, is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking and maintenance of Golgi glycosylation machinery in eukaryotic cells. Mutations in the COG8 gene cause congenital disorder of glycosylation, type IIh, a disease that is characterized by under-glycosylated serum proteins, and whose symptoms include severe psychomotor retardation, failure to thrive, seizures, and dairy and wheat product intolerance.

Forma física

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide

Almacenamiento y estabilidad

For continuous use, store at 2-8 °C for up to one month. For extended storage freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Cláusula de descargo de responsabilidad

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Código de clase de almacenamiento

10 - Combustible liquids

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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COG8 deficiency causes new congenital disorder of glycosylation type IIh
Kranz C, et al.
Human Molecular Genetics, 16(7), 731-741 (2007)
Modeling congenital disorders of N-linked glycoprotein glycosylation in Drosophila melanogaster
Frappaolo A, et al.
Frontiers in Genetics, 9, 436-436 (2018)
Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation
Smith RD and Lupashin VV
Carbohydrate Research, 343(12), 2024-2031 (2008)
Amrita Khakurel et al.
Molecular biology of the cell, 32(17), 1594-1610 (2021-06-24)
The Golgi complex is a central hub for intracellular protein trafficking and glycosylation. Steady-state localization of glycosylation enzymes is achieved by a combination of mechanisms involving retention and recycling, but the machinery governing these mechanisms is poorly understood. Herein we
Farhana Taher Sumya et al.
Traffic (Copenhagen, Denmark), 24(2), 52-75 (2022-12-06)
Conserved Oligomeric Golgi (COG) complex controls Golgi trafficking and glycosylation, but the precise COG mechanism is unknown. The auxin-inducible acute degradation system was employed to investigate initial defects resulting from COG dysfunction. We found that acute COG inactivation caused a

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