SLC2A13 Knockout Cell Line (HEK293)

The choice depends on whether you are studying SLC2A13 (HMIT)'s role as a H⁺-coupled myo-inositol transporter or its emerging functions in neuronal inositol signaling and APP processing in Alzheimer's disease contexts. The Knockout line is the standard tool for asking whether SLC2A13 is required for proton-coupled myo-inositol uptake — HMIT is unique among GLUT family members in transporting inositol rather than hexoses, and unique in coupling transport to a proton gradient rather than facilitative diffusion. Overexpression is useful for testing transport activity in heterologous systems or for studying HMIT's reported role as a binding partner of presenilin and modulator of γ-secretase activity. For HMIT research, the EDITGENE SLC2A13 Knockout in HEK293 is a standard mechanistic platform — HEK293 has been extensively used for HMIT biochemistry and APP/γ-secretase signaling research. Rescue with wild-type or transport-deficient HMIT enables structure-function studies, and is particularly valuable for distinguishing transport function from HMIT's reported scaffolding roles in APP processing.

Primary applications: • Myo-inositol uptake assays: ³H-myo-inositol uptake under varied extracellular pH conditions to characterize HMIT proton-coupled transport (optimal activity at pH 5.0-6.0). • APP processing: amyloid β production analysis (Aβ40/Aβ42 ELISA from conditioned medium) and APP C-terminal fragment analysis given HMIT's reported interaction with the γ-secretase complex. • Inositol phosphate signaling: IP3 and inositol polyphosphate analysis given the contribution of inositol uptake to downstream signaling lipid biosynthesis. • Trafficking studies: HMIT's surface translocation is regulated — imaging analysis of trafficking determinants in rescue cell lines. EDITGENE recommends this model for researchers investigating proton-coupled inositol transport, neuronal inositol biology, and HMIT-mediated APP processing in Alzheimer's disease research.

Yes. HMIT rescue experiments require attention to proton coupling and pH dependence: • Construct design: use a codon-modified SLC2A13 sequence with a small C-terminal tag (FLAG, HA). HMIT has 12 transmembrane domains — N-terminal tags must not disrupt topology. • Transport-deficient rescue: conserved residue mutations in the H⁺ or myo-inositol binding pockets enable structure-function studies — including the conserved aspartate residues critical for proton coupling. • pH-dependence: HMIT transport is highly pH-sensitive, with optimal activity in acidic conditions (pH 5.0-6.0) — rescue assays should be performed under controlled pH conditions. • Functional readout: rescue should restore proton-coupled myo-inositol uptake and, where relevant, modulation of γ-secretase activity on APP substrates. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation for HMIT functional studies.