OSBP Antibodies

Background

OSBP, as an important type of lipid transporter, mainly exists in the Golgi region of eukaryotic cells. This protein mediates the transport and distribution of cholesterol within cells by binding to oxysterol substances, and is also involved in regulating lipid metabolism balance and membrane structure dynamics. During the process of viral infection, OSBP has been confirmed to serve as a host factor required for the replication of various RNA viruses and has attracted much attention due to its crucial role in the assembly of viral replicators. Early research began in the 1980s with the exploration of cholesterol sensing mechanisms. With the breakthrough of cryo-electron microscopy technology, scientists gradually revealed the molecular mechanism by which OSBP mediates bidirectional lipid transport at membrane contact sites in the 2010s. Its unique domain organization and allosteric regulation characteristics provide an important model for understanding the functional evolution of lipid transporters and developing antiviral targeting strategies.

Structure Function Application Advantage Our Products

Structure of OSBP

OSBP is a medium-sized protein with a molecular weight of approximately 95 kDa. This weight may exhibit slight variations across isoforms due to differences in domain composition and post-translational modifications.

Species	Human	Mouse	Bovine	Yeast
Molecular Weight (kDa)	95.2	94.8	94.9	78.6
Primary Structural Differences	Conserved PH, FFAT, and ORD domains	High sequence similarity to human	Minor variations in linker regions	Simplified domain architecture

The OSBP protein contains 807 amino acids and adopts an elongated conformation through its multi-domain architecture. The protein structure features an N-terminal pleckstrin homology (PH) domain that targets membranes, a central two-phenylalanine (FFAT) motif for ER tethering, and a C-terminal oxysterol-binding related domain (ORD) that forms a hydrophobic pocket for lipid transfer. The ORD domain creates a tunnel-like structure capable of shuttling cholesterol between membranes, while regulatory elements control its sterol-sensing and lipid-transfer activities.

Fig. 1 The interaction model between helicase and OSBP is predicted by Alphafold3.¹

Key structural properties of OSBP:

The extension of more structure domain of conformation
PH domain-mediated membrane targeting and localization
Hydrophobic tunnels within the ORD domain are responsible for lipid transport

Functions of OSBP

The core function of the OSBP protein is to regulate the transport and distribution of cholesterol within cells. At the same time, it is also involved in various cellular activities, including the formation of membrane contact sites, viral replication and signal transduction.

Function	Description
Cholesterol transport	Shuttling between the Golgi apparatus and the endoplasmic reticulum to transport cholesterol and maintain membrane lipid homeostasis.
Regulation of phosphatidylinositol	Regulate the phosphoinositol balance on the Golgi membrane through the PI4P/ cholesterol exchange reaction.
Formation of membrane contact sites	The PH domain and FFAT motif were used to connect different organelles to build a lipid exchange platform.
Virus replication support	Hijacked by various RNA viruses as host factors, it is used to construct viral replicators.
Signal pathway regulation	Indirectly affects Hedgehog, mTOR and other key signaling pathways by altering cholesterol distribution.

The lipid exchange mechanism of OSBP exhibits a synergistic anti-transport feature - for each cholesterol molecule output, a PI4P molecule is simultaneously input. This bidirectional transport mode makes it the core regulator of cellular lipid balance.

Applications of OSBP and OSBP Antibody in Literature

1. Olkkonen, Vesa M. "OSBP-related proteins: liganding by glycerophospholipids opens new insight into their function." Molecules 18.11 (2013): 13666-13679. https://doi.org/10.3390/molecules181113666

Studies have shown that OSBP and its related proteins (ORPs/OSBPLs) are a class of lipid transfer proteins that can not only bind to sterols but also specifically bind to phospholipids (such as PI4P and PS). They regulate lipid transport and metabolism through membrane contact sites, and their functions far exceed the scope of their names.

2. Cigler, Marko, et al. "Orpinolide disrupts a leukemic dependency on cholesterol transport by inhibiting OSBP." Nature Chemical Biology 21.2 (2025): 193-202. https://doi.org/10.1038/s41589-024-01614-4

Researchers have discovered that the synthetic compound orpinolide has anti-leukemia activity. The mechanism is to disrupt the homeostasis of the Golgi apparatus, and the direct target is the oxidized steroid-binding protein (OSBP). This study confirmed that sterol transport targeting OSBP is a potential therapeutic strategy for leukemia.

3. Lin, Shaoli, et al. "Oxysterol binding protein (OSBP) contributes to hepatitis E virus replication." Virology Journal 21.1 (2024): 161. https://doi.org/10.1186/s12985-024-02438-3

Research has found that hepatitis E virus (HEV) can interact with the host protein OSBP by using its helicase and hinder the transport of OSBP to the Golgi apparatus. This interaction is crucial for the replication of HEV, revealing a new mechanism by which viruses hijack lipid regulators to promote their own replication.

4. de La Mora, Eugenio, et al. "Nanoscale architecture of a VAP-A-OSBP tethering complex at membrane contact sites." Nature communications 12.1 (2021): 3459. https://doi.org/10.1038/s41467-021-23799-1

The research revealed the structural mechanism by which OSBP collaboratively forms membrane contact sites with endoplasmic reticulum protein VAP.A. The unique "T-shaped" structure formed by the dimer of OSBP effectively Bridges and may promote intermembrane lipid transport.

5. Subramaniyan, Bharathiraja, et al. "Anti-SARS-CoV-2 Small Molecule Targeting of Oxysterol-Binding Protein (OSBP) Activates Cellular Antiviral Innate Immunity." ACS Infectious Diseases 11.5 (2025): 1064-1077. https://doi.org/10.1021/acsinfecdis.4c00631

Research has found that the compound OSW-1 targeting the lipid transporter OSBP can not only broadly inhibit the replication of various justice single-stranded RNA viruses (such as coronaviruses) by reducing the level of OSBP, but also regulate the host's innate immune responses such as type I and type III interferons. This indicates that OSBP is an important node connecting viral replication and cellular immunity.

Creative Biolabs: OSBP Antibodies for Research

Creative Biolabs specializes in the production of high-quality OSBP antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom OSBP Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our OSBP antibodies, custom preparations, or technical support, contact us at email.

Reference

Lin, Shaoli, et al. "Oxysterol binding protein (OSBP) contributes to hepatitis E virus replication." Virology Journal 21.1 (2024): 161. https://doi.org/10.1186/s12985-024-02438-3