DLST Antibodies

Structure of DLST

The DLST gene-encoded dihydrothiolipoamide succinyltransferase is a mitochondrial matrix protein with a molecular weight of approximately 48 kDa. There are moderate molecular weight differences of this protein among different species, mainly due to the evolutionary divergence of its nuclear localization signal sequence and enzyme activity region.

This protein is composed of approximately 450 amino acid residues, and its tertiary structure exhibits the classic E2 core enzyme folding pattern. The core functional domain of the DLST protein contains a thioacyl binding site, which is coupled to the succinyl transfer active center through a flexible lysine residue linking domain. Its active center is composed of a highly conserved histidine - glutamic acid diad, which is responsible for catalyzing the transfer reaction of the thioacyl group. The hydrophobic pocket formed around the active center precisely regulates substrate specificity, ensuring the stability of the tricarboxylic acid cycle metabolic flux.

Fig. 1 Structural Basis of APCDD1L-AS1 Interaction with DLST.¹

Key structural properties of DLST:

• Classical E2 enzyme triple domain folding pattern
• Flexible lysine linker arm with lipoyl binding site
• Conserved histidine - glutamic acid catalytic diad
• Substrate specific hydrophobic pockets maintain the stability of the enzyme active center

Functions of DLST

The core function of the DLST gene-encoded protein is to serve as a key component of the ketoglutarate dehydrogenase complex. It mainly participates in the rate-limiting step of the tricarboxylic acid cycle by catalyzing the succinylation reaction of the thioacyl group.

The catalytic kinetics of this enzyme exhibits typical Mie equation characteristics, and its activity is regulated at multiple levels by substrate concentration, product feedback inhibition and phosphorylation modification, reflecting the precise control mechanism of metabolic hub nodes.

Applications of DLST and DLST Antibody in Literature

1. Shen, Ning, et al. "DLST-dependence dictates metabolic heterogeneity in TCA-cycle usage among triple-negative breast cancer." Communications biology 4.1 (2021): 1289. https://doi.org/10.1038/s42003-021-02805-8

The article indicates that in triple-negative breast cancer, high expression of DLST predicts a poor prognosis for patients. Research has found that inhibiting DLST can specifically suppress the growth of some TNBC cells and promote their death by influencing the tricarboxylic acid cycle and reactive oxygen species pathways, providing a potential therapeutic target for this subtype.

2. Kuhn, Christina, et al. "Candidate drugs associated with sensitivity of cancer cell lines with DLST amplification or high mRNA levels." Oncotarget 14 (2023): 14. https://doi.org/10.18632/oncotarget.28342

Studies have shown that cancer cells with high expression or amplification of DLST are more sensitive to drugs targeting specific pathways. In addition to the known OXPHOS inhibitors, these cells also demonstrated sensitivity to BCL2 inhibitors and multiple ERK/MAPK pathway kinase inhibitors, providing a new potential therapeutic direction for DLST-abnormal tumors.

3. Yang, Rongjin, et al. "Grpel2 maintains cardiomyocyte survival in diabetic cardiomyopathy through DLST-mediated mitochondrial dysfunction: a proof-of-concept study." Journal of translational medicine 21.1 (2023): 200. https://doi.org/10.1186/s12967-023-04049-y

This study reveals for the first time that in diabetic cardiomyopathy, Grpel2 positively regulates the process of its input into mitochondria by interacting with DLST. Overexpression of Grpel2 can improve mitochondrial dysfunction and apoptosis by maintaining DLST function, indicating that it can serve as a potential therapeutic target.

4. Zhang, Quanli, et al. "Hypoxia-inducible APCDD1L-AS1 promotes osimertinib resistance by stabilising DLST to drive tricarboxylic acid cycle in lung adenocarcinoma." Journal of Experimental & Clinical Cancer Research 44.1 (2025): 197. https://doi.org/10.1186/s13046-025-03462-z

This study reveals that in osimertinib-resistant lung adenocarcinoma, hypoxia-induced APCDD1L-AS1 promotes drug resistance by stabilizing the DLST protein and accelerating the tricarboxylic acid cycle. The HIF-1α/APCDD1L-AS1/DLST axis provides a new potential therapeutic target for overcoming drug resistance.

5. Li, Chang, et al. "Case report: A rare DLST mutation in patient with metastatic pheochromocytoma: clinical implications and management challenges." Frontiers in Oncology 14 (2024): 1394552. https://doi.org/10.3389/fonc.2024.1394552

This case report identified a patient with pheochromocytoma carrying a rare germline mutation of the DLST gene. This case presented with multiple metastases after the operation and had a limited response to chemotherapy and other treatments, suggesting that DLST mutations may be associated with the invasiveness and poor prognosis of pheochromocytoma.

Creative Biolabs: DLST Antibodies for Research

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

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