BET1 Antibodies

Structure of BET1

The protein encoded by the BET1 gene has a molecular weight of approximately 22 kDa. There are slight differences among different species, and the specific data are shown in the table below:

This protein is composed of approximately 200 amino acids. Its three-dimensional structure contains a characteristic long intramolecular domain, which mediates protein interactions through a coiled-coil structure. The BET1 protein is located on the surface of the Golgi membrane. Its structure contains a conserved C-terminal transmembrane domain, which anchors the protein to the membrane of transport vesicles. The cytoplasmic region of the protein contains multiple coiled-coil motifs, which form specific hydrophobic regions and mediate the binding with other members of the SNARE complex. The key glutamine residues are located at the center of the SNARE motif, which stabilize the conformation of the fusion complex by forming an ionic layer, thereby precisely regulating the specific recognition and fusion process between vesicles and the target membrane.

Fig. 1 RNA sequencing analysis of the BET1 c.202G>C; p.(Asp68His) missense variant.¹

Key structural properties of BET1:

• The characteristic SNARE coiled-coil domain
• The hydrophobic interface mediates the assembly of protein complexes
• The glutamine residue stabilizes the fusion complex
• The coiled-coil motif in the cytoplasmic region regulates vesicle recognition

Functions of BET1

The main function of the BET1 gene is to mediate the vesicle transport between the endoplasmic reticulum and the Golgi apparatus, playing a central role in the intracellular material transport process. However, it is also involved in various cellular biological processes, including maintaining the structure of the Golgi apparatus and regulating autophagy.

The membrane fusion process mediated by BET1 has strict temporal and spatial specificity. It ensures the accurate targeting of transport vesicles to the Golgi membrane by forming a trans-complex with other SNARE proteins, demonstrating its precise regulatory role in the directional transport of substances within the cell.

Applications of BET1 and BET1 Antibody in Literature

1. Donkervoort, Sandra, et al. "BET1 variants establish impaired vesicular transport as a cause for muscular dystrophy with epilepsy." EMBO Molecular Medicine 13.12 (2021): EMMM202013787. https://doi.org/10.15252/emmm.202013787

This study is the first to reveal that mutations in the BET1 gene cause congenital muscular dystrophy. The variations interfere with the BET1 protein and its interaction with ERGIC-53, causing endoplasmic reticulum-Golgi transport disorders, providing new insights into the disease mechanism.

2. Garcia, Gilberto, et al. "Large‐scale genetic screens identify BET‐1 as a cytoskeleton regulator promoting actin function and life span." Aging Cell 22.1 (2023): e13742. https://doi.org/10.1111/acel.13742

The study found that BET-1 regulates the protection of the actin cytoskeleton through transcription, and delays the functional decline associated with aging. Overexpression of bet-1 in nematodes can maintain the actin function in old age, significantly prolong lifespan and health span, revealing a new mechanism for cytoskeleton homeostasis.

3. Gee, Fiona, et al. "An RNAi-based dimorphic genetic screen identified the double bromodomain protein BET-1 as a sumo-dependent attenuator of RAS-mediated signalling." Plos one 8.12 (2013): e83659. https://doi.org/10.1371/journal.pone.0083659

The study found that BET-1 acts as a substrate for SUMOylation modification and regulates gene expression by physically binding to factors such as SMO-1, thereby inhibiting excessive activation of the RAS/MAPK signaling pathway. This mechanism reveals a new mode of the collaborative interaction between chromatin regulation and SUMOylation.

4. Zhang, Tao, and Wanjin Hong. "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport." Journal of Biological Chemistry 276.29 (2001): 27480-27487. https://doi.org/10.1074/jbc.M102786200

The research has confirmed that Ykt6 is located in the anterograde Golgi apparatus and forms a SNARE complex with proteins such as Bet1, mediating the late fusion of ER-Golgi transport. The functional blockade of Ykt6 leads to fragmentation of the Golgi apparatus, revealing the unique two-stage sequential mechanism of SNARE complex in mammalian cells.

5. Lawal, Bashir, et al. "Transcriptomic-based identification of the immuno-oncogenic signature of cholangiocarcinoma for HLC-018 multi-target therapy exploration." Cells 10.11 (2021): 2873. https://doi.org/10.3390/cells10112873

The research has found that five key genes such as BET1 are highly expressed in cholangiocarcinoma, and they are closely related to tumor immune suppression, metastasis and drug resistance. The small molecule HLC-018 can efficiently bind to these targets, providing a new strategy for the treatment of cholangiocarcinoma.

Creative Biolabs: BET1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality BET1 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom BET1 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 BET1 antibodies, custom preparations, or technical support, contact us at email.