SUB1 Antibodies

Structure of SUB1

The molecular weight of the protein encoded by the SUB1 gene is approximately 14 kDa, and its precise size varies slightly among different species. This protein is composed of 127 amino acids and adopts a conserved β -folding domain as its core structure, forming a typical transcription cofactor folding pattern. Its molecular surface carries a large number of negatively charged amino acid residues, which are responsible for specific interactions with RNA polymerase II and the universal transcription factor TFIIB. The key functional region is located in the acidic activation domain at the C-terminal, which directly participates in the assembly and stabilization of the transcription initiation complex through hydrogen bonds and electrostatic interactions.

Fig. 1 Proposed model of SUB1 and miR-101 regulation in prostate cancer progression.¹

Key structural properties of SUB1:

• The conserved β-fold transcriptional coactivation domain was used
• The surface is rich in acidic amino acid residues
• The C-terminal acidic activation region binds RNA polymerase II and universal transcription factors

Functions of SUB1

The main function of the SUB1 gene is to act as a transcriptional coactivator to participate in the regulation of gene expression and play a key role in DNA damage repair. In addition, it also involves the regulation of cell cycle processes and stress responses.

SUB1 interacts with multiple proteins through its conserved acid-activating domain to precisely regulate the basic transcriptional process in a synergistic manner. The loss of its function may lead to transcriptional abnormalities and genomic instability.

Applications of SUB1 and SUB1 Antibody in Literature

1. Huang, Rongzhong, et al. "The transcription factor SUB1 is a master regulator of the macrophage TLR response in atherosclerosis." Advanced Science 8.19 (2021): 2004162. https://doi.org/10.1002/advs.202004162

This study found that the TLR signaling pathway promotes atherosclerosis through RNA polymerase II coactivator SUB1. Myeline-specific knockout of SUB1 can enhance M2 polarization of macrophages and cholesterol effusion, and reduce plaque formation. Mechanistically, SUB1 activates Irf1 transcription in a CK2-dependent manner, driving the pro-inflammatory M1 phenotype. SUB1 is a key regulatory factor for atherosclerosis induced by TLR.

2. Liu, Gongbao, et al. "ARID1B/SUB1‐activated lncRNA HOXA‐AS2 drives the malignant behaviour of hepatoblastoma through regulation of HOXA3." Journal of cellular and molecular medicine 25.7 (2021): 3524-3536. https://doi.org/10.1111/jcmm.16435

Studies have found that the transcriptional co-activator SUB1 and the chromatin remodeling factor ARID1B jointly regulate the expression of the oncogenic lncRNA HOXA-AS2. This regulatory axis promotes the proliferation, migration and invasion of hepatoblastoma by stabilizing the HOXA3 protein. SUB1 plays a key role in the HoXa-AS2-mediated carcinogenic mechanism, providing a potential target for the treatment of hepatoblastoma.

3. Chakravarthi, Balabhadrapatruni VSK, et al. "MicroRNA-101 regulated transcriptional modulator SUB1 plays a role in prostate cancer." Oncogene 35.49 (2016): 6330-6340. https://doi.org/10.1038/onc.2016.164

Studies have found that the transcriptional co-activator SUB1 is highly expressed in aggressive prostate cancer and is negatively regulated by miR-101. SUB1 promotes its expression by binding to the promoter regions of oncogenes such as PLK1 and C-MYC, driving tumor proliferation and metastasis. Targeting SUB1 or its downstream PLK1 can inhibit tumor growth, revealing the potential of SUB1 as a new therapeutic target for prostate cancer.

4. Martinez, Mariano, et al. "Prodomain-driven enzyme dimerization: a pH-dependent autoinhibition mechanism that controls Plasmodium Sub1 activity before merozoite egress." Mbio 15.3 (2024): e00198-24. https://doi.org/10.1128/mbio.00198-24

Research has found that Plasmodium protease SUB1 regulates its spatiotemporal activation through a unique PH-dependent dimerization mechanism. Under acidic conditions, its original domain promotes the formation of inactive homodimers. It dissociates into active monomers in a neutral pH environment. This regulatory mechanism precisely controls the multi-step maturation process of SUB1 under the action of the aspartic acid protease PmX, and ultimately mediates the key step of the release of schizozoites from infected red blood cells.

5. Lidumniece, Elina, et al. "Peptidic boronic acids are potent cell-permeable inhibitors of the malaria parasite egress serine protease SUB1." Proceedings of the National Academy of Sciences 118.20 (2021): e2022696118. https://doi.org/10.1073/pnas.2022696118

Research is conducted to develop new inhibitors targeting the key protease SUB1 of the malaria parasite. This boric acid compound can effectively inhibit SUB1 activity, prevent the egress process of the parasite from red blood cells, and significantly suppress the proliferation of parasites. Such inhibitors are expected to become new antimalarial drugs with both preventive and therapeutic effects.

Creative Biolabs: SUB1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SUB1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SUB1 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 SUB1 antibodies, custom preparations, or technical support, contact us at email.