UBQLN2 Antibodies

Structure of UBQLN2

UBQLN2 is a multi-domain protein with a molecular weight of approximately 60 kDa. Its precise molecular weight may vary due to transcript subtypes and post-translational modifications. This protein is composed of the following main domains:

The UBQLN2 protein is composed of 574 amino acid residues, and its primary structure contains multiple functional modules. The core feature of the protein lies in the ubiquitin-like domain at the N-terminal and the ubiquitin-related domain at the C-terminal, which jointly mediate the interaction with ubiquitination substrates. This protein exhibits a typical modular structure, with its secondary structure mainly composed of α-helicles and connecting ring regions, forming a flexible scaffold capable of binding to multiple substrates. The STM region located at the C-terminal (amino acids 518-524) is crucial for the self-aggregation of proteins and liquid-liquid phase separation behavior. Pathogenic mutations in this region can significantly disrupt its normal phase separation kinetics, leading to abnormal protein aggregation, which is closely related to the occurrence of neurodegenerative diseases.

Fig. 1 Schematic of UBQLN2 and amyotrophic lateral sclerosis (ALS)-associated mutations.¹

Key structural properties of UBQLN2:

• Modular multi-domain architecture
• Ubiquitin-like and ubiquitin-related domains that mediate substrate recognition
• C-terminal STM low-complexity regions that regulate liquid-liquid phase separation behavior

Functions of UBQLN2

The core function of the UBQLN2 protein is to participate in the quality control of intracellular proteins. However, this protein also plays a key role in various cellular processes, especially in maintaining protein homeostasis and signal transduction.

UBQLN2 achieves functional diversity through its multi-domain characteristics. Unlike myoglobin, which has a specific oxygen-binding curve, the functional flexibility of UBQLN2 mainly results from the complexity of its domain combination and post-translational modifications, enabling it to adapt to various cellular stress conditions and exert corresponding protective effects.

Applications of UBQLN2 and UBQLN2 Antibody in Literature

1. Matthews, Autumn M., and Alexandra M. Whiteley. "UBQLN2 in neurodegenerative disease: mechanistic insights and emerging therapeutic potential." Biochemical Society Transactions 53.04 (2025): 823-833. https://doi.org/10.1042/BST20253053

The article indicates that mutations in the UBQLN2 gene can impair its function of transporting abnormal proteins to the proteasome for degradation, leading to protein accumulation and subsequently causing degeneration of motor neurons, which is closely related to the pathogenesis of amyotrophic lateral sclerosis (ALS).

2. Renaud, Laurence, et al. "Key role of UBQLN2 in pathogenesis of amyotrophic lateral sclerosis and frontotemporal dementia." Acta neuropathologica communications 7.1 (2019): 103. https://doi.org/10.1186/s40478-019-0758-7

The article indicates that mutations in the UBQLN2 gene can impair its mediated abnormal protein clearance function, leading to the formation of intrusions in the cytoplasm and affecting processes such as stress granules, ultimately driving the occurrence of neurodegenerative diseases such as ALS/FTD.

3. Chen, Tianhong, et al. "UBQLN2 promotes the production of type I interferon via the TBK1-IRF3 pathway." Cells 9.5 (2020): 1205. https://doi.org/10.3390/cells9051205

Research has found that UBQLN2 can interact with TBK1, enhancing its activity and promoting the phosphorylation of IRF3 and the production of interferon. ALS/ FTD-related mutations can weaken this effect, leading to the dysregulation of the TBK1-IRF3 pathway, which may be a new mechanism of neurodegeneration.

4. Wang, Jia-Lin, et al. "Silencing UBQLN2 Enhances the Radiosensitivity of Esophageal Squamous Cell Carcinoma (ESCC) via Activating p38 MAPK." Journal of Oncology 2023.1 (2023): 2339732. https://doi.org/10.1155/2023/2339732

Research has found that high expression of UBQLN2 in esophageal squamous cell carcinoma predicts a poor prognosis. Mechanically, inhibiting UBQLN2 can significantly enhance the radiosensitivity of esophageal squamous cell carcinoma by activating the p38 MAPK signaling pathway and inhibiting the phosphorylation of DNA-PKcs, and is expected to become a new target for radiotherapy sensitization.

5. Kim, Sang Hwa, et al. "Axon guidance genes modulate neurotoxicity of ALS-associated UBQLN2." Elife 12 (2023): e84382. https://doi.org/10.7554/eLife.84382

Research has found that both fruit fly and human motor neuron models have confirmed that UBQLN2 mutations lead to protein aggregation and synaptic defects, and their neurotoxicity can be alleviated by inhibiting the Unc-5/DCC pathway, suggesting that growth cone dysregulation is the key pathogenic mechanism.

Creative Biolabs: UBQLN2 Antibodies for Research

Creative Biolabs specializes in the production of high-quality UBQLN2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom UBQLN2 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 UBQLN2 antibodies, custom preparations, or technical support, contact us at email.