TRAK1 Antibodies
Background
TRAK1, as a linker protein, is mainly present in the cytoplasm of neurons. This protein interacts with various molecules and participates in regulating the transport and distribution of mitochondria, thereby ensuring the normal functioning of energy supply and signal transmission in neurons. TRAK1 plays a crucial role in the formation and functional maintenance of neural synapses, and its abnormal function is closely related to the occurrence and development of certain neurological diseases. This gene was first discovered and identified in related molecular research, and the protein encoded by it is closely linked to transport systems such as kinesin and dynein. This provides an important foundation for understanding the mechanism of intracellular substance transport. The complex formed by TRAK1 interacting with Miro protein and others has been proven to be a key molecular module regulating mitochondrial movement, and it plays an indispensable role in the survival and functional maintenance of neurons.
Structure of TRAK1
The TRAK1 protein exhibits relatively conserved structural features across different species, but there are minor differences in its molecular weight. The molecular weight of this protein is approximately 90 to 100 kDa. This difference mainly results from the subtle variations in the amino acid sequences of each species.
| Species | Human | Mouse | Rat | Fruit fly |
| Molecular Weight (kDa) | 97.6 | 97.3 | 97.5 | 95.8 |
| Primary Structural Differences | Contains typical adaptor protein domain | Has high homology with humans | Has a few variations in the N-terminal region | Relatively simplified structure, retaining core functional domains |
The TRAK1 protein has multiple subtypes, and its typical subtype consists of nearly 900 amino acids. The overall structure of this protein presents a slender coiled-coil conformation, and it is connected to the dynamin/driver protein transport complex through the binding region of its N-terminal GTPase domain. The coiled-coil domain in the middle part of the TRAK1 protein mediates homodimerization, while the Miro binding domain at its C-terminus is responsible for interacting with the Miro protein that anchors to the outer mitochondrial membrane. The coiled-coil region of TRAK1 constitutes the protein scaffold, stabilizing the entire molecular structure, and multiple functional sites within it coordinate the binding with different transport proteins, thus ensuring the directed movement of mitochondria within the cell.
Fig. 1 Location of TRAK1 variant sites in patients with epilepsy.1
Key structural properties of TRAK1:
- The coiled-coil domain mediates the formation of homodimers
- The N-terminal region is responsible for binding to microtubule transport motor proteins
- Multiple coiled-coil repeat sequences constitute the protein scaffold
- The C-terminal Miro binding domain enables mitochondrial anchoring
Functions of TRAK1
The main function of TRAK1 is to regulate the transport and distribution of mitochondria within the cell. Additionally, this protein is involved in various cellular physiological processes, including maintaining mitochondrial homeostasis and regulating the autophagy process.
| Function | Description |
| Mitochondrial Transport | As a linker protein, TRAK1 connects mitochondria with microtubule motor proteins and mediates the bidirectional movement of mitochondria along microtubules. |
| Neuron Distribution Regulation | Regulates the localization of mitochondria within the axons and dendrites of neurons, ensuring the energy supply at the synaptic sites. |
| Maintenance of mitochondrial homeostasis | Participates in the transportation and clearance of damaged mitochondria, and cooperates with the autophagy pathway to regulate mitochondrial quality. |
| Calcium signal regulation | By interacting with the Miro protein, it responds to changes in intracellular calcium signals and regulates mitochondrial movement. |
| Neurodevelopmental Support | During the processes of neuronal differentiation, axon growth, and synapse formation, ensure the precise distribution of mitochondria. |
The binding mechanism of TRAK1 to microtubule motor proteins is highly specific, which is significantly different from the cage-like structure assembly process of clathrin. This reflects that TRAK1, as a bridging protein, plays a unique localization function in mitochondrial transport.
Applications of TRAK1 and TRAK1 Antibody in Literature
1. Li, Ren-Ke, et al. "Role of TRAK1 variants in epilepsy: genotype–phenotype analysis in a pediatric case of epilepsy with developmental disorder." Frontiers in Molecular Neuroscience 17 (2024): 1342371. https://doi.org/10.3389/fnmol.2024.1342371
This study is the first to reveal that the double allelic variation of TRAK1 can lead to epilepsy and developmental disorders. Most of the affected children present with infantile spasms and are prone to developing into status epilepticus, with a high mortality rate. Early treatment can improve the prognosis. Valproic acid combined with adrenocorticotropic hormone is effective.
2. Henrichs, Verena, et al. "Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments." Nature communications 11.1 (2020): 3123. https://doi.org/10.1038/s41467-020-16972-5
This study found that TRAK1, as a mitochondrial transport adapter protein, can directly bind to microtubules, helping to drive protein-1 to bypass obstacles through the Tau island and enhance its robustness in moving in crowded environments, thereby ensuring efficient mitochondrial transport.
3. Lee, Crystal A., Lih-Shen Chin, and Lian Li. "Hypertonia-linked protein Trak1 functions with mitofusins to promote mitochondrial tethering and fusion." Protein & cell 9.8 (2018): 693-716. https://doi.org/10.1007/s13238-017-0469-4
This study found that TRAK1 interacts with mitochondrial fusion proteins and promotes mitochondrial fusion. Its absence leads to fragmentation of mitochondria, while mutations related to dystonia disrupt this function, suggesting that abnormal mitochondrial dynamics are associated with the pathogenesis of this disease.
4. Onodera, Yasuhito, et al. "Arf6-driven cell invasion is intrinsically linked to TRAK1-mediated mitochondrial anterograde trafficking to avoid oxidative catastrophe." Nature communications 9.1 (2018): 2682. https://doi.org/10.1038/s41467-018-05087-7
The study found that the Arf6-AMAP1 pathway regulates the localization of ILK, blocks the mitochondrial retrograde transport mediated by RhoT1-TRAK1, and achieves the forward distribution of mitochondria to support cell invasion while avoiding the generation of harmful reactive oxygen species.
5. Ogawa, Fumiaki, et al. "DISC1 complexes with TRAK1 and Miro1 to modulate anterograde axonal mitochondrial trafficking." Human molecular genetics 23.4 (2014): 906-919. https://doi.org/10.1093/hmg/ddt485
The study found that DISC1 participates in mitochondrial anterograde transport by binding to TRAK1 and Miro1. The psychotic risk variant DISC1-37W disrupts this function, leading to abnormal mitochondrial distribution, suggesting that mitochondrial transport disorders may increase the risk of mental illness.
Creative Biolabs: TRAK1 Antibodies for Research
Creative Biolabs specializes in the production of high-quality TRAK1 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 TRAK1 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 TRAK1 antibodies, custom preparations, or technical support, contact us at email.
Reference
- Li, Ren-Ke, et al. "Role of TRAK1 variants in epilepsy: genotype–phenotype analysis in a pediatric case of epilepsy with developmental disorder." Frontiers in Molecular Neuroscience 17 (2024): 1342371. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3389/fnmol.2024.1342371
Anti-TRAK1 antibodies
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- AActivation
- AGAgonist
- APApoptosis
- BBlocking
- BABioassay
- BIBioimaging
- CImmunohistochemistry-Frozen Sections
- CIChromatin Immunoprecipitation
- CTCytotoxicity
- CSCostimulation
- DDepletion
- DBDot Blot
- EELISA
- ECELISA(Cap)
- EDELISA(Det)
- ESELISpot
- EMElectron Microscopy
- FFlow Cytometry
- FNFunction Assay
- GSGel Supershift
- IInhibition
- IAEnzyme Immunoassay
- ICImmunocytochemistry
- IDImmunodiffusion
- IEImmunoelectrophoresis
- IFImmunofluorescence
- IGImmunochromatography
- IHImmunohistochemistry
- IMImmunomicroscopy
- IOImmunoassay
- IPImmunoprecipitation
- ISIntracellular Staining for Flow Cytometry
- LALuminex Assay
- LFLateral Flow Immunoassay
- MMicroarray
- MCMass Cytometry/CyTOF
- MDMeDIP
- MSElectrophoretic Mobility Shift Assay
- NNeutralization
- PImmunohistologyp-Paraffin Sections
- PAPeptide Array
- PEPeptide ELISA
- PLProximity Ligation Assay
- RRadioimmunoassay
- SStimulation
- SESandwich ELISA
- SHIn situ hybridization
- TCTissue Culture
- WBWestern Blot




