Analytical Data
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Gene name
LAT1
- Application
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Alternative Names
CD98; MDU1; 4T2HC; 4F2; NACAE; SLC7A5; MPE16; Solute Carrier Family 7 Member 5; Cationic Amino Acid Transporter,y+ System; L-Type Amino Acid Transporter
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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
Q01650
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Expression Region
Met1~Asn49
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Molecular Weight
26kDa
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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
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Protein Description
LAT1, or L-type amino acid transporter 1, is a key protein involved in the transport of large neutral amino acids across cell membranes. Its significance has surged in recent years due to its role in various physiological and pathological processes, including cancer development, neurobiology, and metabolic disorders. LAT1 is often overexpressed in many tumors, facilitating the uptake of amino acids that promote cell growth and proliferation, making it a potential target for cancer therapy. Research has shown that inhibiting LAT1 can hinder tumor growth and enhance the efficacy of existing chemotherapy agents. Moreover, LAT1 is critical for nutrient sensing and neuronal signaling, indicating its importance in brain function and development. The study of LAT1's structure and function has been further propelled by advances in molecular biology techniques, enabling detailed characterization of its transport mechanisms and regulatory pathways. Understanding LAT1's roles could lead to novel therapeutic strategies for treating diseases related to abnormal amino acid metabolism and enhance our knowledge of nutrient transport systems in general. As ongoing studies aim to elucidate the precise molecular interactions and signaling pathways involving LAT1, the implications of this research are vast, encompassing everything from basic science to potential clinical applications in disease management.
