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Description
LAT1-4F2hc Flag & His tag Protein, Human (Detergent)Product Specification Species Human Synonyms LAT1 4F2hc Accession NM_003486. 7NM_001012662. 2 Amino Acid Sequence LAT1: Ala2 Thr507 with Flag Tag at the N Terminus 4F2hc: Glu2 Ala631 with His Tag at the N Terminus Expression System HEK293 Molecular Weight LAT1: 35 40kDa (Reducing) 4F2hc: 90 130kDa (Reducing) Purity 90% by SDS PAGE Conjugation Unconjugated Physical Appearance Liquid Storage Buffer 50mM Hepes, 150mM NaCl, 0. 02% GDN, pH8. 0 Stability &
Product Specification
| Species | Human |
| Synonyms | LAT1-4F2hc |
| Accession | NM_003486.7、NM_001012662.2 |
| Amino Acid Sequence | LAT1: Ala2-Thr507 with Flag Tag at the N-Terminus |
| Expression System | HEK293 |
| Molecular Weight | LAT1:35-40kDa (Reducing) 4F2hc:90-130kDa (Reducing) |
| Purity | ＞90% by SDS-PAGE |
| Conjugation | Unconjugated |
| Physical Appearance | Liquid |
| Storage Buffer | 50mM Hepes, 150mM NaCl, 0.02% GDN, pH8.0 |
| Stability & Storage | ·6 months from date of receipt, -60 to -80 °C as supplied. |
| Reference | 1.Bhakuni T, Norden PR, Ujiie N, Tan C, Lee SK, Tedeschi T, Hsieh YW, Wang Y, Liu T, Fawzi AA, Kume T. FOXC1 regulates endothelial CD98 (LAT1/4F2hc) expression in retinal angiogenesis and blood-retina barrier formation. Nat Commun. 2024 May 16;15(1):4097. |
Background
LAT1 (SLC7A5) is an essential amino acid transporter that forms a heterodimer with 4F2hc (SLC3A2). The recently resolved cryo-EM structure reveals a critical "outward-facing occluded conformation," where inhibitors bind to the classical substrate-binding pocket, with their tails specifically wedged between the substrate-binding site and transmembrane domain TM10. This provides atomic-level details for understanding its transport and inhibition mechanisms. LAT1 is not only responsible for transporting essential amino acids but also mediates the transmembrane influx of neuropathic pain drugs such as gabapentin. Additionally, by interacting with voltage-gated potassium channels (Kv1.1/Kv1.2) and sodium channels (Nav1.7), it regulates neuronal excitability and plays a central role in nociceptive transmission. LAT1 is highly expressed in various tumors, making it a potential target for anticancer drug design. At the same time, its upregulation in pain pathways of the dorsal root ganglia and spinal cord, along with its close association with mTOR signaling, the Wnt/β-catenin pathway, and T/B cell-related pain, positions it not only as a novel target for alleviating neuropathic pain (e.g., by mediating the uptake of first-line drugs) but also as a key structural foundation for developing new drugs capable of crossing the blood-brain barrier while exerting analgesic effects.
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