Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
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SLC13A5 (solute carrier family 13 member 5), also known as NaCT, encodes a multi-pass transmembrane sodium-coupled citrate transporter predominantly localized to the plasma membrane. This transporter is expressed in multiple tissues, with prominent expression in the liver and detectable expression in nervous-system-related tissues and other organs. Distinct from soluble intracellular proteins, each SLC13A5 protomer contains 11 transmembrane helices and conserved structural elements involved in sodium and citrate coordination. Structural studies indicate that SLC13A5 assembles as a homodimer in the membrane. Its primary function is to mediate Na⁺-dependent transport of citrate across the plasma membrane, thereby linking extracellular citrate availability to intracellular carbon metabolism and related metabolic processes. Reduced SLC13A5 expression or impaired transporter activity may decrease cellular citrate uptake and alter downstream metabolic pathways. Rather than functioning mainly through heteromeric membrane-partner complexes, SLC13A5 activity depends on its transporter architecture, sodium coupling, substrate recognition, and membrane localization. Sequence or expression changes affecting these properties may therefore influence citrate transport and associated cellular metabolic responses.
Sequence‑level alterations to the SLC13A5 locus may compromise the structural organisation of assembled plasma‑membrane transporter‑partner complexes and alter readouts derived from cell‑surface molecular interaction events. Closely related members of SLC13‑type solute‑carrier subfamily cannot fully replicate the complete set of SLC13A5‑dependent behaviours during heteromeric transporter‑complex formation and stable integration within plasma‑membrane assemblies. Shifts in SLC13A5 protein levels often align with cellular demands for membrane‑solute‑related activities, making this protein a useful research target to explore sodium‑coupled citrate‑transporter activities and membrane‑solute‑balance molecular dynamics. Predominantly distributed at plasma‑membrane together with minor intracellular membrane fractions, SLC13A5 contributes to heteromeric transporter‑complex formation and does not sustain persistent substrate translocation without appropriate physiological stimulus triggering. Its multi‑modular twelve‑transmembrane SLC13‑family transporter architecture with cytoplasmic regulatory domains distinguishes this membrane glycoprotein from many other membrane‑embedded surface components; such structural features support the maintenance of membrane‑transporter complex arrangement and permit selective physical contacts with cell‑surface binding partners. Diminished functional performance of SLC13A5 may disturb the proper arrangement of plasma‑membrane transporter assemblies and weaken endogenous cellular adaptive buffering capacity, further supporting its research value for studies focused on sodium‑coupled citrate‑transporter subunits.
Fig. 1 Structural features of human SLC13A5 multi-pass transmembrane transporter, illustrating transmembrane topology and cytoplasmic N-/C-terminal domains for membrane-partner subunit interaction.1
The biological functions of transmembrane SLC13A5 transporter protein are focused on sustained heteromeric partner-complex interaction and plasma-membrane-homeostasis coordination:
Creative Biolabs offers purified SLC13A5 membrane samples produced under unified preparation workflows, including full-length SLC13A5 constructs and isolated domain variants. Truncated domain fragments cannot support complete surface-partner-complex assembly behaviours, while full-length constructs suit research focused on transporter-subunit-partner interaction and plasma-membrane anchoring functional observation. All batches receive uniform quality screening. Functional-relevant observation may only be carried out with full-length samples under simulated plasma-membrane microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis across separate test groups. Full-length SLC13A5 samples retain intact partner-interaction-domain conformation after standardized purification, which supports reliable detection of weak and transient subunit-partner contacts for comparative functional analysis.
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Creative Biolabs provides adjustable SLC13A5 expression cell research models with varied expression levels, applicable to structural observation of multi-pass transmembrane sodium-coupled citrate-transporter proteins and research into membrane-partner molecular interaction. Sample evaluation includes sustained target expression detection and preliminary partner-interaction observation, enabling side-by-side comparison of subunit-binding behaviours under differing expression abundances. These cell systems can pair with diverse laboratory analysis schemes to track changes in partner-assembly efficiency alongside shifting target protein levels.
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Anti-SLC13A5 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for plasma-membrane localization mapping and identification of subunit-partner molecular complexes. The antibody series can work alongside common laboratory detection reagents to realize multi-dimensional observation of target distribution within membrane-enriched sample materials.
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Beyond catalog products, Creative Biolabs offers specialized custom services for SLC13A5 research:
SLC13A5 might act as a multi-pass transmembrane sodium-coupled citrate-transporter subunit protein and participate in heteromeric plasma-membrane complex assembly to modulate membrane-transporter-complex arrangement and plasma-membrane homeostasis.
SLC13A5 expression status could alter membrane-partner-complex assembly efficiency and local plasma-membrane-coupled molecular-interaction balance, serving as a major transporter mediator of membrane-solute-homeostasis-associated biological processes.
No, SLC13A5-associated research reagents from Creative Biolabs are exclusively built for exploring membrane-transporter-dependent plasma-membrane solute-regulatory mechanisms, and shall not be deployed for any clinical-oriented workflows. These preparations are optimized for basic laboratory investigation and do not satisfy performance benchmarks required for clinical implementation.
Offerings include full-length SLC13A5 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on plasma-membrane homeostasis and membrane-transporter-mediated membrane-partner perception.
Laboratory observation schemes may include subunit-partner interaction related tests to analyse molecular-binding associated behaviors under simulated plasma-membrane environments.
