cogc-2 Antibody
Description
Definition and Biological Role of COG2
COG2 is part of the COG complex, an eight-subunit (COG1–COG8) tethering machinery that regulates vesicular trafficking and glycosylation enzyme localization within the Golgi apparatus . Depletion or mutation of COG2 disrupts:
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Glycosylation: Altered terminal galactosylation and sialylation of glycoproteins .
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Vesicle tethering: Impaired retrograde transport of Golgi-resident enzymes like MGAT1 (mannosyl-glycoprotein acetylglucosaminyltransferase) and MAN2A1 (mannosidase α class 2A member 1) .
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Cellular pathology: Linked to congenital disorders of glycosylation (CDG), characterized by multi-organ dysfunction .
COG2 Antibody Characteristics
Commercial COG2 antibodies (e.g., CAB6251, HPA076994) are rabbit polyclonal antibodies validated for applications such as Western blotting and immunofluorescence . Key features include:
Research Findings on COG2 Depletion
Studies using COG2 antibodies have revealed critical insights:
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Glycosylation defects: COG2-deficient cells show increased binding of Galanthus nivalis lectin (GNL) and Griffonia simplicifolia lectin-II (GS-II), indicating exposed terminal mannose and GlcNAc residues due to defective glycosylation .
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Vesicle accumulation: Depletion causes Golgi enzymes to mislocalize to COPI-coated vesicular structures, disrupting glycosylation .
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Functional interplay: COG2 interacts with tethering factors (e.g., p115) and SNARE proteins to regulate intra-Golgi trafficking .
Table 1: Impact of COG2 Knockdown on Glycosylation Markers
| Lectin | Binding Target | Change in COG2-Deficient Cells |
|---|---|---|
| Wheat Germ Agglutinin (WGA) | Sialic acid/GlcNAc | Reduced binding (↓ sialylation) |
| GS-II | GlcNAc/agalactosylated N-glycans | Increased binding |
| GNL | Terminal mannose | Increased binding |
Applications in Disease Research
COG2 antibodies are pivotal in:
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Diagnosing CDG: Detecting COG2 mislocalization in patient fibroblasts .
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Studying neurodegeneration: COG2 dysfunction correlates with impaired protein trafficking in models of Parkinson’s and Alzheimer’s diseases .
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Viral infection studies: Golgi glycosylation defects impact viral entry mechanisms (e.g., SARS-CoV-2) .
Challenges and Future Directions
Product Specs
Composition: 50% Glycerol, 0.01M Phosphate Buffered Saline (PBS), pH 7.4
Target Background
Q&A
FAQs for Researchers on Antibody Research Methodologies (Generalized Framework)
Note: While "cogc-2 Antibody" is not directly referenced in available literature, this FAQ adopts a generalized approach based on antibody research principles from peer-reviewed sources.
Advanced Research Questions
How to resolve contradictions in neutralization data across viral variants?
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Strategy:
What methods identify broadly neutralizing antibodies against conserved epitopes?
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Workflow:
How to optimize antibody engineering for enhanced therapeutic efficacy?
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Key considerations:
