Analytical Data
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Gene name
LAMTOR1
- Application
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Alternative Names
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1 Lipid raft adaptor protein p18 Protein associated with DRMs and endosomes p27Kip1-releasing factor from RhoA Short name: p27RF-Rho
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6IAA8
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Expression Region
2-161aa
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Molecular Weight
21.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
LAMTOR1, also known as late endosomal/lysosomal adaptor, MAPK and mTOR activator 1, is a crucial protein that plays a significant role in the regulation of mTOR signaling pathway, which is essential for cell growth, proliferation, and metabolism. Research has highlighted LAMTOR1's function as an adaptor protein that facilitates the assembly of the mTORC1 complex at lysosomal membranes, thereby influencing nutrient sensing and autophagy processes. The dysregulation of mTOR signaling has been implicated in various diseases, including cancer, metabolic disorders, and neurodegenerative conditions, making LAMTOR1 a potential therapeutic target. Studies have shown that LAMTOR1 interacts with several key proteins involved in cellular signaling, including Rag GTPases, which are essential for mTORC1 activation in response to amino acids and other growth factors. The recombinant production of LAMTOR1 protein enables detailed studies of its structure and function, providing insights into its role in cellular signaling pathways. Understanding the molecular mechanisms underpinning LAMTOR1's function could lead to novel therapeutic strategies for diseases linked to mTOR dysregulation. Moreover, characterizing LAMTOR1 as a recombinant protein allows researchers to elucidate its interactions with other signaling components, paving the way for innovative drug design and therapeutic interventions aimed at restoring normal signaling pathways in disease contexts. Thus, the study of LAMTOR1 and its recombinant protein forms represents a significant advance in our understanding of cellular signaling and its implications for human health.
