USP30 Antibodies

Structure of USP30

The protein encoded by the USP30 gene has a relative molecular mass of approximately 55 kDa. The USP30 proteins from different species have certain differences in molecular weight, which mainly results from the species-specificity of their amino acid sequences.

The USP30 protein is composed of approximately 500 amino acids. Its spatial structure is formed by the folding of multiple domains, resulting in a characteristic three-dimensional conformation. The catalytic core of this protein is located at the carboxyl terminus and contains a conserved cysteine box and histidine box, jointly constituting the typical active center of the deubiquitinating enzyme. Surrounding the catalytic domain, there are multiple α-helices and β-sheet structures, which maintain the conformational stability of the active site through hydrophobic interactions. The amino terminus contains a transmembrane helix structure, which anchors USP30 to the outer mitochondrial membrane. The two key residues near the active site - cysteine and histidine - respectively participate in the nucleophilic attack and proton transfer processes, jointly mediating the hydrolysis reaction of the ubiquitin chain.

Fig. 1 Structure, regulation, and molecular characteristics of USP30.¹

Key structural properties of USP30:

• C-terminal catalytic domain,
• N-terminal transmembrane helix,
• Ubiquitin binding region,
• Peripheral regulatory loop, which controls enzyme activity and substrate selectivity

Functions of USP30

The main function of USP30 is to regulate mitochondrial autophagy and the ubiquitin signaling pathway. However, it is also involved in various cellular biological processes, including protein homeostasis maintenance and oxidative stress response.

The enzyme activity curve of USP30 exhibits typical Michaelis-Menten kinetic characteristics, which is consistent with the catalytic behavior of most deubiquitinating enzymes. This indicates that it has a high affinity and specific hydrolytic function towards ubiquitin substrates.

Applications of USP30 and USP30 Antibody in Literature

1. Wang, Feng, et al. "USP30: structure, emerging physiological role, and target inhibition." Frontiers in Pharmacology 13 (2022): 851654. https://doi.org/10.3389/fphar.2022.851654

The article indicates that USP30 is a deubiquitinating enzyme localized in mitochondria, which regulates mitochondrial autophagy, apoptosis and tumor metabolism by cleaving Lys6 ubiquitin chains. Its abnormality is related to neurodegenerative diseases and cancer. Various inhibitors have been developed, and some have entered the preclinical research stage. This article summarizes its structure, function and inhibitor progress.

2. Fang, Tracy-Shi Zhang, et al. "Knockout or inhibition of USP30 protects dopaminergic neurons in a Parkinson's disease mouse model." Nature Communications 14.1 (2023): 7295. https://doi.org/10.1038/s41467-023-42876-1

The article indicates that the absence or inhibition of USP30 can alleviate the motor disorders in Parkinson's disease model mice, reduce the pathological accumulation of αSynuclein, and protect dopaminergic neurons. The study suggests that inhibiting USP30 may become a new modulating therapy for Parkinson's disease.

3. Zhang, Ruohan, et al. "USP30 inhibition augments mitophagy to prevent T cell exhaustion." Science Advances 11.33 (2025): eadv6902. https://doi.org/10.1126/sciadv.adv6902

The article indicates that USP30 is highly expressed in CD8+ T cells that have been depleted. It impairs the function of these cells by inhibiting mitochondrial autophagy. Targeted inhibition of USP30 can restore mitochondrial health and T cell activity, thereby enhancing anti-tumor immunity. Studies have shown that USP30 is a potential therapeutic target for reversing T cell exhaustion.

4. Okarmus, Justyna, et al. "USP30 inhibition induces mitophagy and reduces oxidative stress in parkin-deficient human neurons." Cell Death & Disease 15.1 (2024): 52. https://doi.org/10.1038/s41419-024-06439-6

The article indicates that USP30 inhibition can promote mitochondrial autophagy in PARK2-deficient neurons derived from Parkinson's disease patients, reduce oxidative stress, and improve cell status. Research shows that USP30 inhibitors are expected to become drugs for treating neurological diseases related to mitochondrial dysfunction.

5. Du, Jiapeng, et al. "Spotlight on USP30: structure, function, disease and target inhibition." Frontiers in Pharmacology 16 (2025): 1629709. https://doi.org/10.3389/fphar.2025.1629709

The article indicates that USP30 participates in the progression of tumors and neurodegenerative diseases by regulating mitochondrial autophagy and stabilizing cancer proteins, etc. Inhibiting USP30 can reverse the malignant phenotype of tumors and exert neuroprotective effects, making it a highly promising therapeutic target. This article summarizes the research progress on its structure, function and inhibitors.

Creative Biolabs: USP30 Antibodies for Research

Creative Biolabs specializes in the production of high-quality USP30 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 USP30 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 USP30 antibodies, custom preparations, or technical support, contact us at email.