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Anti rab27a

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Anti-Rab27A is a specific antibody that recognizes the Rab27A protein. Rab27A is a small GTPase involved in the regulation of vesicle trafficking and exocytosis. The Anti-Rab27A antibody can be used to detect and study the expression and localization of Rab27A in various cell and tissue samples.

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Lab products found in correlation

Precast polyacrylamide gel, by Bio-Rad (3 mentions) Anti calnexin, by Thermo Fisher Scientific (3 mentions) V3 western workflow, by Bio-Rad (3 mentions) Anti cd63, by Thermo Fisher Scientific (3 mentions) Ripa lysis and extraction buffer, by Thermo Fisher Scientific (3 mentions) Goat peroxidase conjugated anti mouse igg secondary anti body, by Bio-Rad (2 mentions) Anti hcmv capsid mcp, by Bio-Rad (2 mentions) Anti mouse monoclonal antibodies clones, by Bio-Rad (2 mentions) Anti tsg101, by Thermo Fisher Scientific (1 mentions)

3 protocols using anti rab27a

1

EV and HCMV Protein Characterization

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Total proteins were extracted from both EV and HCMV fractions, according to RIPA Lysis and Extraction Buffer (Thermo Fisher Scientific, Waltham, MA). 10 μg of proteins were loaded on a 4–20% precast polyacrylamide gel (Bio-Rad Laboratories, Hercules, CA) and separated by SDS-PAGE, then transferred to PVDF membranes and probed with anti-CD63 (1 μg/ml, Thermo Fisher Scientific, Waltham, MA), anti-Calnexin (1 μg/ml, Thermo Fisher Scientific, Waltham, MA), anti-Rab27A (1 μg/ml, Thermo Fisher Scientific, Waltham, MA), anti-HCMV capsid MCP (2 μg/ml), and anti-HCMV tegument pp150 (2 μg/ml) monoclonal primary anti-mouse monoclonal antibodies (clones 28–4 and 36–14) and then goat peroxidase-conjugated anti-mouse IgG secondary anti-body (Bio-Rad Laboratories, Hercules, CA). Peroxidase activity and digital images were detected by using V3 Western Workflow™ (Bio-Rad Laboratories, Hercules, CA).
Zicari S., Arakelyan A., Palomino R.A., Fitzgerald W., Vanpouille C., Lebedeva A., Schmitt A., Bomsel M., Britt W, & Margolis L. (2018). Human cytomegalovirus-infected cells release extracellular vesicles that carry viral surface proteins. Virology, 524, 97-105.
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2

Extracellular Vesicle Protein Profile Analysis

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Total proteins were extracted from EV pellets with RIPA Lysis and Extraction Buffer (Thermo Fisher Scientific, Waltham, MA). 10 μg of proteins were loaded on a 4–20% precast polyacrylamide gel (Bio-Rad Laboratories, Hercules, CA) and separated by SDS-PAGE, then transferred to PVDF membranes. Proteins were detected with anti-CD63, anti-Rab27A, anti-TSG101 and anti-Calnexin (Thermo Fisher Scientific), followed by species specific horse-radish peroxidase labeled antibodies (Bio-Rad) and signal detection by V3 Western Workflow™ (Bio-Rad).
MERCURIO V., FITZGERALD W., MOLODTSOV I, & MARGOLIS L. (2020). Persistent immune activation in HIV-1 infected ex vivo model tissues subjected to antiretroviral therapy: Soluble and extracellular vesicle-associated cytokines. Journal of acquired immune deficiency syndromes (1999), 84(1), 45-53.
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3

EV and HCMV Protein Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Total proteins were extracted from both EV and HCMV fractions, according to RIPA Lysis and Extraction Buffer (Thermo Fisher Scientific, Waltham, MA). 10 μg of proteins were loaded on a 4–20% precast polyacrylamide gel (Bio-Rad Laboratories, Hercules, CA) and separated by SDS-PAGE, then transferred to PVDF membranes and probed with anti-CD63 (1 μg/ml, Thermo Fisher Scientific, Waltham, MA), anti-Calnexin (1 μg/ml, Thermo Fisher Scientific, Waltham, MA), anti-Rab27A (1 μg/ml, Thermo Fisher Scientific, Waltham, MA), anti-HCMV capsid MCP (2 μg/ml), and anti-HCMV tegument pp150 (2 μg/ml) monoclonal primary anti-mouse monoclonal antibodies (clones 28–4 and 36–14) and then goat peroxidase-conjugated anti-mouse IgG secondary anti-body (Bio-Rad Laboratories, Hercules, CA). Peroxidase activity and digital images were detected by using V3 Western Workflow™ (Bio-Rad Laboratories, Hercules, CA).
Zicari S., Arakelyan A., Palomino R.A., Fitzgerald W., Vanpouille C., Lebedeva A., Schmitt A., Bomsel M., Britt W, & Margolis L. (2018). Human cytomegalovirus-infected cells release extracellular vesicles that carry viral surface proteins. Virology, 524, 97-105.
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