MPST Antibodies

Structure of MPST

The MPST gene encodes a thiosulfate sulfur transferase with a relative molecular mass of approximately 33 kDa. The molecular weights of MPST proteins from different species vary to some extent, which is mainly due to the subtle differences in amino acid sequences.

The thiosulfate sulfur transferase encoded by the MPST gene consists of 297 amino acids and its three-dimensional structure presents a compact spherical folding pattern. This protein is composed of two domains, each of which contains a conserved active site cysteine residue (Cys248), which forms a thiosulfate intermediate during the catalytic process. The active center of the enzyme protein is located in the hydrophobic gap between the two domains, and this conformation is conducive to substrate binding and sulfur atom transfer reactions. The secondary structure of MPST is mainly composed of α-helices and β-sheets, among which the β-sheets form the core framework, and the α-helices are arranged around it to form a stable catalytic environment. The arginine residue (Arg187) near the active site stabilizes the substrate through electrostatic interactions, while the aspartic acid residue (Asp182) participates in the proton transfer process, jointly ensuring the catalytic efficiency of the enzyme.

Fig. 1 Organization and reaction catalyzed by MPST.¹

Key structural properties of MPST:

• A globular fold composed of two domains
• A conserved cysteine active site (Cys248)
• Hydrophobic gaps forming a substrate binding pocket
• Arginine and aspartic acid residues participating in the catalytic reaction

Functions of MPST

The thiosulfate sulfur transferase encoded by the MPST gene is mainly involved in sulfur metabolism and cyanide detoxification processes, and also plays a role in various physiological reactions, including hydrogen sulfide production and regulation of redox balance.

The enzyme kinetics curve of the MPST gene follows the typical Michaelis equation. Unlike the allosteric regulation characteristic of hemoglobin, it shows a high substrate affinity as a sulfur transferase and plays a rapid catalytic role in cyanide detoxification.

Applications of MPST and MPST Antibody in Literature

1. Yadav, Pramod Kumar, et al. "Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations." Journal of Biological Chemistry 295.19 (2020): 6299-6311. https://doi.org/10.1074/jbc.RA120.012616

The article indicates that MPST catalyzes sulfur transfer to produce H₂S, and there is no difference in the kinetic characteristics of its two shear variants, MPST1 and MPST2. The study found that changes in the concentration of thioredoxin can significantly regulate the reaction rate and direction of MPST, cysteine is an important physiological sulfur receptor, while N-acetylcysteine is not an effective substrate.

2. Katsouda, Antonia, et al. "CTH/MPST double ablation results in enhanced vasorelaxation and reduced blood pressure via upregulation of the eNOS/sGC pathway." Frontiers in pharmacology 14 (2023): 1090654. https://doi.org/10.3389/fphar.2023.1090654

The article indicates that the MPST and CTH double knockout mice have lower blood pressure and enhanced vasodilation in response to acetylcholine. The study found that long-term deficiency of endogenous H₂S induces adaptive upregulation of the eNOS/sGC pathway, revealing a new regulatory relationship between H₂S and the NO signaling pathway.

3. Xi, Xiaoyu, et al. "SLC2A1 and MPST as diagnostic and prognostic biomarkers of potential endometrial cancer." Frontiers in immunology 16 (2025): 1575916. https://doi.org/10.3389/fimmu.2025.1575916

The article indicates that the SLC2A1 and MPST genes have diagnostic and prognostic value in endometrial cancer. Their expression is associated with immune infiltration and TP53, and the methylation status of the CpG island affects prognosis, providing a new direction for targeted therapy of endometrial cancer.

4. Latorre, Jessica, et al. "The combined partial knockdown of CBS and MPST genes induces inflammation, impairs adipocyte function-related gene expression and disrupts protein persulfidation in human adipocytes." Antioxidants 11.6 (2022): 1095. https://doi.org/10.3390/antiox11061095

The article indicates that the combined knockdown of CBS and MPST in fat cells reduces the level of protein sulfhydryl groups, alters fat production, mitochondrial biosynthesis, and the expression of inflammation-related genes, suggesting that these two enzymes are crucial for maintaining the function of fat cells.

5. Tao, Beibei, et al. "3-mercaptopyruvate sulfurtransferase, not cystathionine β-synthase nor cystathionine γ-lyase, mediates hypoxia-induced migration of vascular endothelial cells." Frontiers in pharmacology 8 (2017): 657. https://doi.org/10.3389/fphar.2017.00657

The article indicates that hypoxia (10% O₂) promotes the migration of vascular endothelial cells by upregulating the MPST protein, while CSE and CBS do not have this effect. The expression of MPST is regulated post-transcriptionally, and RNA-binding proteins such as nucleolin may be involved in the regulation of its mRNA 3'-UTR region.

Creative Biolabs: MPST Antibodies for Research

Creative Biolabs specializes in the production of high-quality MPST 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 MPST 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 MPST antibodies, custom preparations, or technical support, contact us at email.