TMEM106B Antibodies

Background

TMEM106B encodes a transmembrane protein that is mainly expressed in the endosomes-lysosomes system of neurons, and participates in regulating the size, transport, and functional homeostasis of lysosomes. This protein maintains the balance of protein degradation and organelle stability in neurons through interactions with various lysosomal proteins, and is crucial for the long-term health of the nervous system. In 2010, the first genome-wide association study identified common variations of the TMEM106B gene as associated with the risk of frontotemporal dementia. Its single nucleotide polymorphisms can affect lysosomal activity and the pathological process of neurodegeneration. Further studies have further revealed its regulatory role in aging-related neurodegenerative diseases (such as Alzheimer's disease, Parkinson's disease), becoming a key molecular target for understanding the mechanisms of lysosomal dysfunction and neuronal degeneration.

Structure Function Application Advantage Our Products

Structure of TMEM106B

TMEM106B is a transmembrane protein with a molecular weight of approximately 32 kDa. The molecular weight of this protein is relatively conserved among different mammalian species, with the main differences arising from the sequence polymorphism of its encoding gene and post-transcriptional modifications.

Species	Human	Mouse	Rat	Nonhuman Primate
Molecular Weight (kDa)	~32	~31.8	~31.9	~32.1
Primary Structural Differences	The C-terminal domain is highly conserved, while the N-terminal part is variable.	High sequence similarity in the transmembrane region	There are phosphorylation sites in the cytoplasmic tail region.	Homology with human protein sequences

This protein is composed of 274 amino acids and its primary structure includes an N-terminal signal peptide, a single transmembrane domain, and a longer C-terminal cytoplasmic tail region. The secondary structure of TMEM106B is mainly composed of α-helices, among which the transmembrane domain forms a crucial hydrophobic helix that anchors it to the endosome/lysosome membrane. Its tertiary structure folds to form a functional transmembrane protein, with the C-terminal domain exposed in the cytoplasm, which can interact with various effector proteins including MAP6 and FIG4, thereby regulating the transport, acidification, and size of lysosomes. The dysfunction of this protein is closely related to frontotemporal lobar degeneration and other neurodegenerative diseases associated with aging.

Fig. 1 Structure, physiological and pathologic function of TMEM106B.¹

Key structural properties of TMEM106B:

Single transmembrane helical domain
The C-terminal cytoplasmic tail region contains multiple functional domains.
Highly conservative palmitoylation sites regulate subcellular localization

Functions of TMEM106B

The main function of the TMEM106B gene is to regulate the homeostasis and transport of the endosome-lysosome system. However, it is also involved in various cellular physiological processes, including neuroprotection, aging regulation, and membrane dynamics control.

Function	Description
Lysosome Function Regulation	Maintain the size, acidity and enzyme activity of lysosomes, which affects the intracellular degradation and recycling processes.
Maintenance of Neuronal Homeostasis	Regulating the transport of cellular organelles and the clearance of protein aggregates within neurons is crucial for the long-term survival of neurons.
Aging Regulation	The imbalance in TMEM106B levels is closely associated with cellular aging and the risk of aging-related neurodegenerative diseases (such as frontotemporal lobar degeneration).
Membrane Transport Regulation	By influencing the transport pathways of endosomes - late endosomes - lysosomes, it participates in intracellular membrane vesicle transport and cargo sorting.
Stress Response	Under cellular stress conditions (such as protein toxicity stress), it helps maintain lysosomal function and protects the cell from damage.

The functional expression of TMEM106B depends on its precise subcellular localization and protein interaction network. Studies have shown that its expression level and genetic polymorphisms significantly affect the efficiency of lysosomal function, and are highly correlated with the age of onset and progression rate of neurodegenerative diseases, which reveals its core role as a key regulator of cellular homeostasis.

Applications of TMEM106B and TMEM106B Antibody in Literature

1. Zhu, Min, et al. "Physiological and pathological functions of TMEM106B in neurodegenerative diseases." Cellular and Molecular Life Sciences 81.1 (2024): 209. https://doi.org/10.1007/s00018-024-05241-z

The article indicates that the transmembrane protein TMEM106B is a key regulator of lysosomal function, and its mutations can accelerate the progression of neurodegenerative diseases. Recent studies have revealed that its C-terminal can form amyloid fibers, providing a new direction for the elucidation of the mechanisms of related diseases and targeted treatment.

2. Baggen, Jim, et al. "TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry." Cell 186.16 (2023): 3427-3442. https://doi.org/10.1016/j.cell.2023.06.005

The research has found that the lysosomal protein TMEM106B can serve as an alternative receptor for the novel coronavirus SARS-CoV-2 besides ACE2, facilitating the virus' entry and fusion with the cell. Its specific antibody can prevent infection, revealing a new mechanism for the virus' invasion.

3. Jiao, Hai-Shan, Peng Yuan, and Jin-Tai Yu. "TMEM106B aggregation in neurodegenerative diseases: linking genetics to function." Molecular Neurodegeneration 18.1 (2023): 54. https://doi.org/10.1186/s13024-023-00644-1

The research has found that mutations in the TMEM106B gene can promote the formation of amyloid fibril aggregates of its protein, interfere with normal functions and cause lysosomal dysfunction. This reveals a new mechanism for neurodegenerative diseases and provides potential therapeutic targets for them.

4. Takahashi, Hideyuki, and Stephen M. Strittmatter. "The role of endolysosomal progranulin and TMEM106B in neurodegenerative diseases." Molecular Neurodegeneration 20.1 (2025): 86. https://doi.org/10.1186/s13024-025-00873-6

The research has found that TMEM106B and the precursor of granular protein play a crucial role in neurodegenerative diseases. The amyloid fibrils formed by them and the regulation of glycosphingolipids reveal common pathological pathways across different diseases, providing new targets for the development of broad-spectrum therapeutic strategies.

5. Bacioglu, Mehtap, et al. "Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems." Acta neuropathologica communications 12.1 (2024): 99. https://doi.org/10.1186/s40478-024-01813-z

The research found that the TMEM106B protein, after being cleaved, can form amyloid fiber deposits in the brain, dorsal root ganglia, and spinal cord, especially being enriched in astrocytes and lysosome-related structures. This suggests that its deposition has tissue specificity and is associated with organelles.

Creative Biolabs: TMEM106B Antibodies for Research

Creative Biolabs specializes in the production of high-quality TMEM106B antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom TMEM106B 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 TMEM106B antibodies, custom preparations, or technical support, contact us at email.

Reference

Zhu, Min, et al. "Physiological and pathological functions of TMEM106B in neurodegenerative diseases." Cellular and Molecular Life Sciences 81.1 (2024): 209. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.1007/s00018-024-05241-z