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Merck
CN

SAB4200427

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

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

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

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, IP, WB
Citations:
6

Key Documents

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biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~70 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

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

UniProt accession no.

Q96MW5

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... COG8(84342)

General description

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.

Immunogen

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

Application

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

Biochem/physiol Actions

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

Physical form

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

Preparation Note

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.

Disclaimer

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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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

常规特殊物品
低风险生物材料
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Certificates of Analysis (COA)

Lot/Batch Number
012M4808

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Modeling congenital disorders of N-linked glycoprotein glycosylation in Drosophila melanogaster
Frappaolo A, et al.
Frontiers in Genetics, 9, 436-436 (2018)
COG8 deficiency causes new congenital disorder of glycosylation type IIh
Kranz C, et al.
Human Molecular Genetics, 16(7), 731-741 (2007)
Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation
Smith RD and Lupashin VV
Carbohydrate Research, 343(12), 2024-2031 (2008)
Comparative analyses of the Conserved Oligomeric Golgi (COG) complex in vertebrates
Quental R, et al.
BMC Evolutionary Biology, 10(1), 212-212 (2010)
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
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