PRDM1 Antibodies

Structure of PRDM1

The molecular weight of the protein encoded by the PRDM1 gene is approximately 92 kDa, and its precise value varies among different species. For specific data, please refer to the table below：

This protein is composed of multiple functional domains: although the PR/SET domain at the N-terminal lacks histone methyltransferase activity, it participates in protein-protein interactions; The central proline-rich region mediates transcriptional inhibitory function; The C-terminal contains five C2H2-type zinc finger structures, which are responsible for the recognition and binding of specific DNA sequences. Its secondary structure is mainly α -helix, which, together with β -folding, forms a stable spatial conformation. The zinc finger module coordinates with zinc ions through conserved cysteine and histidine residues to form fingered protrusions, which precisely embed into the DNA grooves for target gene regulation. This multi-domain structure enables it to recruit histone modification complexes, which play a core regulatory role in the terminal differentiation of B cells.

Fig. 1 Protein structures of PRDM1α and PRDM1β.¹

Key structural properties of PRDM1:

• Transcription factor modules composed of multiple domains
• N-terminal PR/SET domain mediated protein interaction but had no catalytic activity
• The C-terminal zinc finger array achieves DNA-specific recognition through ββα folding
• Proline enrichment region formed intramolecular interaction interface regulation of transcription

Functions of PRDM1

The core function of the PRDM1 gene is to act as the "master regulatory switch" for cell differentiation, but its mechanism of action covers a multi-level immune regulatory network:

This gene achieves functional specificity through a "synergistic inhibition circuit" : its zinc finger domain recognizes a specific palindromic sequence (5'-GAAAGGCAA-3') in the promoter of the target gene, while the N-terminal inhibition domain recruits chromatin remodeling complexes, forming a positive feedback regulatory circuit. This dual-lock mechanism ensures precise control over the fate transformation of immune cells under conditions such as cell stress, differentiation signals, or oncogenic mutations. Its functional disorders are closely related to diseases such as diffuse large B-cell lymphoma and systemic lupus erythematosus.

Applications of PRDM1 and PRDM1 Antibody in Literature

1. Li, Qing, et al. "PRDM1/BLIMP1 induces cancer immune evasion by modulating the USP22-SPI1-PD-L1 axis in hepatocellular carcinoma cells." Nature communications 13.1 (2022): 7677. https://doi.org/10.1038/s41467-022-35469-x

The article indicates that PRDM1 in liver cancer can promote the expression of PD-L1, induce T cell exhaustion, and weaken its own anti-cancer effect. Studies have shown that the combination of PD-1 blockade can enhance the therapeutic effect, providing a new combined treatment approach for such patients.

2. Hu, Xing, et al. "PHLDA1-PRDM1 mediates the effect of lentiviral vectors on fate-determination of human retinal progenitor cells." Cellular and Molecular Life Sciences 81.1 (2024): 305. https://doi.org/10.1007/s00018-024-05279-z

Research has found that lentiviral vectors activate PRDM1 by up-regulating PHLDA1, leading to abnormal differentiation of retinal progenitor cells into photoreceptors. Inhibiting the PHLDA1-PRDM1 axis can avoid this risk, providing a safe new strategy for gene therapy of congenital eye diseases.

3. Guo, Huidong, et al. "PRDM1 drives human primary T cell hyporesponsiveness by altering the T cell transcriptome and epigenome." Frontiers in Immunology 13 (2022): 879501. https://doi.org/10.3389/fimmu.2022.879501

Studies have revealed that low expression of PRDM1 is associated with acute graft-versus-host disease. PRDM1 can serve as a key factor, inducing low T cell response through epigenetic regulation and promoting Treg amplification, providing a new target for the prevention and treatment of aGVHD.

4. Jin, Han, et al. "Identification of a PRDM1-regulated T cell network to regulate atherosclerotic plaque inflammation." Genome Medicine 17.1 (2025): 1-22. https://doi.org/10.1186/s13073-025-01541-6

Research has found that the down-regulation of PRDM1 expression in T cells within plaques can exacerbate atherosclerosis. This factor constitutes a key protective network, and its absence leads to plaque instability, making it a potential therapeutic target.

5. Zhou, Bo, et al. "A potential prognostic marker PRDM1 in pancreatic adenocarcinoma." Journal of Oncology 2022.1 (2022): 1934381. https://doi.org/10.1155/2022/1934381

Research has found that PRDM1 is highly expressed in pancreatic cancer. Its methylation modification, the tumor-related pathways it regulates, and its association with immune cell infiltration jointly promote cancer and lead to a poor prognosis, making it a potential biomarker and therapeutic target.

Creative Biolabs: PRDM1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality PRDM1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom PRDM1 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 PRDM1 antibodies, custom preparations, or technical support, contact us at email.