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.
HighlightsGet a real taste of Creative Biolabs, one of the most professional custom service providers in the world. We are committed to providing highly customized comprehensive solutions with the best quality to advance your projects.
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Loading...All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
Solute carrier family 7 member 1 (SLC7A1) is a multi-spanning integral membrane amino acid transporter encoded by the SLC7A gene family, widely distributed on plasma membranes of epithelial and connective tissue cell populations. The protein features fourteen continuous transmembrane helices that assemble to form substrate permeation cavities, paired with small cytoplasmic N- and C-terminal regulatory segments without large extracellular ligand binding folds. It mediates bidirectional exchange transport of cationic amino acid substrates across lipid bilayers, relying on electrochemical gradients to drive substrate translocation under standard cellular metabolic conditions. Intracellular pools of arginine, lysine and related cationic amino acids rely on balanced SLC7A1 transport activity to sustain polypeptide synthesis and nitrogen metabolism pathways; insufficient transporter abundance leads to depleted cytoplasmic substrate reserves that slow basal biosynthetic processes across cell types. Different tissue layers establish distinct amino acid gradient magnitudes, and SLC7A1 transport kinetics adjust to match local substrate supply and consumption rates, preventing extreme accumulation or depletion of cationic amino acids within cytoplasmic compartments. Conserved polar residues lining the central translocation cavity support selective recognition of positively charged amino acid side chains while restricting transit of neutral and anionic small molecule substrates, forming the structural basis for substrate selectivity of this carrier protein.
Variants within SLC7A1 transmembrane coding regions might alter cavity residue composition and weaken cationic amino acid selectivity or slow substrate translocation turnover rates, which correlates with disrupted intracellular nitrogen metabolism in tissue model systems. Other SLC7 paralogs carry partial amino acid transport capacity but cannot fully replicate SLC7A1’s broad cationic substrate spectrum and gradient coupling mechanism. SLC7A1 fully integrates into plasma lipid bilayers and cannot detach into soluble cytoplasmic protein pools without complete membrane architecture breakdown. Its multi-helix integral topology separates substrate permeation cavities from cytoplasmic regulatory tails, granting the transporter dual potential to tune cellular amino acid uptake and efflux rates according to transmembrane charge gradients. Persistent loss of functional SLC7A1 tends to unbalance cytoplasmic cationic amino acid reserves and restrain steady-state protein synthesis activity, making this solute carrier a suitable research object for amino acid transport and metabolic homeostasis analysis.
Fig. 1 Two-dimensional topology of mouse CAT1 (SLC7A1) showing transmembrane architecture and key residues. The diagram illustrates the arrangement of transmembrane segments with intracellular N- and C-termini, and highlights conserved amino acid residues within the substrate translocation pathway.1
The biological functions of integral membrane SLC7A1 amino acid transporter are focused on charged substrate capture and electrochemical gradient coupled shuttling:
Creative Biolabs offers purified SLC7A1 membrane protein samples produced under unified preparation workflows, including full-length SLC7A1 constructs and isolated transmembrane cavity domain variants. Truncated fragments cannot support complete cationic amino acid recognition and gradient-coupled transit activity, while full-length constructs fit cellular amino acid metabolism research. All batches receive uniform quality screening. Functional assessments may only be performed under simulated lipid bilayer microenvironment setups. Transmembrane cavity structural features are preserved across batches to support comparative substrate binding analysis between experimental groups. Full-length SLC7A1 membrane samples retain intact polar substrate coordination residues after standardized purification, which supports reliable detection of weak and transient amino acid-cavity binding events in comparative membrane functional analysis.
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Creative Biolabs provides cell research models with adjustable SLC7A1 expression levels, suitable for structural observation of multi-helix solute carriers and amino acid metabolism research. Sample assessment covers sustained target membrane expression detection and preliminary substrate binding analysis, enabling side-by-side comparison of amino acid transit behavior under varying SLC7A1 abundances. These cell models can be paired with metabolite quantification schemes to track cytoplasmic amino acid pool shifts linked to transporter dosage changes.
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Anti-SLC7A1 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for epithelial cell membrane localization mapping and transporter complex identification. The antibody series works with common laboratory detection reagents to support multi-dimensional observation of SLC7A1 distribution within tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for SLC7A1 research:
SLC7A1 may act as multi-spanning solute carrier to mediate gradient-coupled bidirectional transport of cationic amino acids across cell membranes.
SLC7A1 expression status might adjust cellular amino acid reserve levels, serving as a key mediator of cytoplasmic nitrogen homeostasis biological processes.
No, all SLC7A1 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material design and functional screening are optimized exclusively for basic laboratory research, without meeting clinical application criteria.
Offerings include full-length SLC7A1 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on cationic amino acid transport.
Laboratory analysis schemes may include charged amino acid binding assays to assess substrate coordination capacity under simulated lipid bilayer environments.
